Q60675 · LAMA2_MOUSE
- ProteinLaminin subunit alpha-2
- GeneLama2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3118 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLaminin subunit alpha-2
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ60675
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Major component.
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 135 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MPAATAGILLLLLLGTLEG | ||||||
Chain | PRO_0000017057 | 20-3118 | Laminin subunit alpha-2 | |||
Sequence: SQTQRRQSQAHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQPVRNPQCRICNQNSSNPYQRHPITNAIDGKNTWWQSPSIKNGVEYHYVTITLDLQQVFQIAYVIVKAANSPRPGNWILERSLDDVEYKPWQYHAVTDTECLTLYNIYPRTGPPSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDPSPELLEFTSARYIRLRFQRIRTLNADLMMFAHKDPREIDPIVTRRYYYSVKDISVGGMCICYGHARACPLDPATNKSRCECEHNTCGESCDRCCPGFHQKPWRAGTFLTKSECEACNCHGKAEECYYDETVASRNLSLNIHGKYIGGGVCINCTHNTAGINCETCVDGFFRPKGVSPNYPRPCQPCHCDPTGSLSEVCVKDEKYAQRGLKPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNCSGLGSTNEDPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGCEECFCSGVSNRCQSSYWTYGNIQDMRGWYLTDLSGRIRMAPQLDNPDSPQQISISNSEARKSLLDGYYWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTEKILQLMIIFEGNDLRISTAYKEVYLEPSEEHIEEVSLKEEAFTIHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIFRLSSVNLESAVPYPTDRRIATDVEVCQCPPGYSGSSCETCWPRHRRVNGTIFGGICEPCQCFAHAEACDDITGECLNCKDHTGGPYCNECLPGFYGDPTRGSPEDCQPCACPLNIPSNNFSPTCHLDRSLGLICDECPIGYTGPRCERCAEGYFGQPSIPGGSCQPCQCNDNLDYSIPGSCDSLSGSCLICKPGTTGRYCELCADGYFGDAVNAKNCQPCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQLGRGCLPCNCNSFGSKSFDCEASGQCWCQPGVAGKKCDRCAHGYFNFQEGGCIACDCSHLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGCKVCNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDCFLPGTDATTCDLETRKCSCSDQTGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGCSSCYCFGVTSQCSEAKGLIRTWVTLSDEQTILPLVDEALQHTTTKGIAFQKPEIVAKMDEVRQELHLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGTPTHARIITRHMAAPLIGQLTRHEIEMTEKEWKYYGDDPRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGHVLAGSPPAHLIERCDCPPGYSGLSCETCAPGFYRLRSEPGGRTPGPTLGTCVPCQCNGHSSQCDPETSVCQNCQHHTAGDFCERCALGYYGIVRGLPNDCQPCACPLISPSNNFSPSCVLEGLEDYRCTACPRGYEGQYCERCAPGYTGSPSSPGGSCQECECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAECVFCGDECTGLLLGDLARLEQMTMNINLTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCVRTYRPEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVRALDGPKASMVPSTYHSVSPPGYTILDVDANAMLFVGGLTGKIKKADAVRVITFTGCMGETYFDNKPIGLWNFREKEGDCKGCTVSPQVEDSEGTIQFDGEGYALVSRPIRWYPNISTVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHNDGKWKAFTLSRIQKQANISIVDIDSNQEENVATSSSGNNFGLDLKADDKIYFGGLPTLRNLSMKARPEVNVKKYSGCLKDIEISRTPYNILSSPDYVGVTKGCSLENVYTVSFPKPGFVELAAVSIDVGTEINLSFSTRNESGIILLGSGGTLTPPRRKRRQTTQAYYAIFLNKGRLEVHLSSGTRTMRKIVIKPEPNLFHDGREHSVHVERTRGIFTVQIDEDRRHMQNLTEEQPIEVKKLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINSIPMDFAQPIAFKNADIGRCTYQKPREDESEAVPAEVIVQPQPVPTPAFPFPAPTMVHGPCVAESEPALLTGSKQFGLSRNSHIAIAFDDTKVKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDGQWHKIKIVRVKQEGILYVDDASSQTISPKKADILDVVGILYVGGLPINYTTRRIGPVTYSLDGCVRNLHMEQAPVDLDQPTSSFHVGTCFANAESGTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRPTGVLLGVSSQKMDGMGIEMIDEKLMFHVDNGAGRFTAIYDAGIPGHMCNGQWHKVTAKKIKNRLELVVDGNQVDAQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKLTKGTGKPLEVNFAKALELRGVQPVSCPTT | ||||||
Glycosylation | 51 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 85 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 283↔292 | |||||
Sequence: CICYGHARAC | ||||||
Disulfide bond | 285↔303 | |||||
Sequence: CYGHARACPLDPATNKSRC | ||||||
Glycosylation | 299 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 305↔314 | |||||
Sequence: CEHNTCGESC | ||||||
Disulfide bond | 317↔337 | |||||
Sequence: CCPGFHQKPWRAGTFLTKSEC | ||||||
Disulfide bond | 340↔349 | |||||
Sequence: CNCHGKAEEC | ||||||
Disulfide bond | 342↔374 | |||||
Sequence: CHGKAEECYYDETVASRNLSLNIHGKYIGGGVC | ||||||
Glycosylation | 359 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 376 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 377↔386 | |||||
Sequence: CTHNTAGINC | ||||||
Disulfide bond | 389↔407 | |||||
Sequence: CVDGFFRPKGVSPNYPRPC | ||||||
Disulfide bond | 410↔422 | |||||
Sequence: CHCDPTGSLSEVC | ||||||
Disulfide bond | 412↔438 | |||||
Sequence: CDPTGSLSEVCVKDEKYAQRGLKPGSC | ||||||
Disulfide bond | 440↔449 | |||||
Sequence: CKTGFGGVNC | ||||||
Disulfide bond | 452↔462 | |||||
Sequence: CVRGYHGYPDC | ||||||
Disulfide bond | 465↔478 | |||||
Sequence: CNCSGLGSTNEDPC | ||||||
Glycosylation | 466 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 467↔482 | |||||
Sequence: CSGLGSTNEDPCVGPC | ||||||
Disulfide bond | 484↔493 | |||||
Sequence: CKENVEGEDC | ||||||
Disulfide bond | 496↔511 | |||||
Sequence: CKSGFFNLQEDNQKGC | ||||||
Glycosylation | 742 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 753↔762 | |||||
Sequence: CQCFAHAEAC | ||||||
Disulfide bond | 755↔769 | |||||
Sequence: CFAHAEACDDITGEC | ||||||
Disulfide bond | 772↔781 | |||||
Sequence: CKDHTGGPYC | ||||||
Disulfide bond | 784↔800 | |||||
Sequence: CLPGFYGDPTRGSPEDC | ||||||
Disulfide bond | 803↔818 | |||||
Sequence: CACPLNIPSNNFSPTC | ||||||
Disulfide bond | 805↔828 | |||||
Sequence: CPLNIPSNNFSPTCHLDRSLGLIC | ||||||
Disulfide bond | 831↔840 | |||||
Sequence: CPIGYTGPRC | ||||||
Disulfide bond | 843↔858 | |||||
Sequence: CAEGYFGQPSIPGGSC | ||||||
Disulfide bond | 861↔875 | |||||
Sequence: CQCNDNLDYSIPGSC | ||||||
Disulfide bond | 863↔882 | |||||
Sequence: CNDNLDYSIPGSCDSLSGSC | ||||||
Disulfide bond | 885↔894 | |||||
Sequence: CKPGTTGRYC | ||||||
Disulfide bond | 897↔911 | |||||
Sequence: CADGYFGDAVNAKNC | ||||||
Disulfide bond | 914↔926 | |||||
Sequence: CRCNINGSFSEIC | ||||||
Disulfide bond | 916↔933 | |||||
Sequence: CNINGSFSEICHTRTGQC | ||||||
Glycosylation | 919 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 935↔944 | |||||
Sequence: CRPNVQGRHC | ||||||
Disulfide bond | 947↔960 | |||||
Sequence: CKPETFGLQLGRGC | ||||||
Disulfide bond | 963↔975 | |||||
Sequence: CNCNSFGSKSFDC | ||||||
Disulfide bond | 965↔981 | |||||
Sequence: CNSFGSKSFDCEASGQC | ||||||
Disulfide bond | 983↔992 | |||||
Sequence: CQPGVAGKKC | ||||||
Disulfide bond | 995↔1007 | |||||
Sequence: CAHGYFNFQEGGC | ||||||
Disulfide bond | 1010↔1019 | |||||
Sequence: CDCSHLGNNC | ||||||
Disulfide bond | 1012↔1026 | |||||
Sequence: CSHLGNNCDPKTGQC | ||||||
Disulfide bond | 1028↔1037 | |||||
Sequence: CPPNTTGEKC | ||||||
Glycosylation | 1031 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1040↔1053 | |||||
Sequence: CLPNTWGHSIVTGC | ||||||
Disulfide bond | 1056↔1068 | |||||
Sequence: CNCSTVGSLASQC | ||||||
Glycosylation | 1057 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1058↔1075 | |||||
Sequence: CSTVGSLASQCNVNTGQC | ||||||
Disulfide bond | 1077↔1086 | |||||
Sequence: CHPKFSGMKC | ||||||
Disulfide bond | 1089↔1099 | |||||
Sequence: CSRGHWNYPLC | ||||||
Disulfide bond | 1102↔1114 | |||||
Sequence: CDCFLPGTDATTC | ||||||
Disulfide bond | 1104↔1130 | |||||
Sequence: CFLPGTDATTCDLETRKCSCSDQTGQC | ||||||
Disulfide bond | 1132↔1141 | |||||
Sequence: CKVNVEGVHC | ||||||
Disulfide bond | 1144↔1159 | |||||
Sequence: CRPGKFGLDAKNPLGC | ||||||
Disulfide bond | 1378↔1387 | |||||
Sequence: CPPGYSGLSC | ||||||
Disulfide bond | 1416↔1425 | |||||
Sequence: CQCNGHSSQC | ||||||
Disulfide bond | 1418↔1432 | |||||
Sequence: CNGHSSQCDPETSVC | ||||||
Disulfide bond | 1435↔1444 | |||||
Sequence: CQHHTAGDFC | ||||||
Disulfide bond | 1447↔1462 | |||||
Sequence: CALGYYGIVRGLPNDC | ||||||
Disulfide bond | 1465↔1480 | |||||
Sequence: CACPLISPSNNFSPSC | ||||||
Disulfide bond | 1467↔1490 | |||||
Sequence: CPLISPSNNFSPSCVLEGLEDYRC | ||||||
Disulfide bond | 1493↔1502 | |||||
Sequence: CPRGYEGQYC | ||||||
Disulfide bond | 1505↔1520 | |||||
Sequence: CAPGYTGSPSSPGGSC | ||||||
Disulfide bond | 1523↔1535 | |||||
Sequence: CECDPYGSLPVPC | ||||||
Disulfide bond | 1525↔1542 | |||||
Sequence: CDPYGSLPVPCDRVTGLC | ||||||
Disulfide bond | 1544↔1553 | |||||
Sequence: CRPGATGRKC | ||||||
Disulfide bond | 1556↔1567 | |||||
Sequence: CEHWHAREGAEC | ||||||
Disulfide bond | 1570 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 1574 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 1593 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1610 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1696 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1806 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1897 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1912 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1916 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2013 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2024 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2041 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2122 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2236 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2298↔2324 | |||||
Sequence: CMGETYFDNKPIGLWNFREKEGDCKGC | ||||||
Glycosylation | 2356 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2431 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2474 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2491↔2517 | |||||
Sequence: CLKDIEISRTPYNILSSPDYVGVTKGC | ||||||
Glycosylation | 2547 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2554 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2644 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2679↔2706 | |||||
Sequence: CVWNLVINSIPMDFAQPIAFKNADIGRC | ||||||
Glycosylation | 2889 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2905↔2930 | |||||
Sequence: CVRNLHMEQAPVDLDQPTSSFHVGTC | ||||||
Disulfide bond | 3083↔3115 | |||||
Sequence: CIRSLKLTKGTGKPLEVNFAKALELRGVQPVSC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-282 | Laminin N-terminal | ||||
Sequence: QQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQPVRNPQCRICNQNSSNPYQRHPITNAIDGKNTWWQSPSIKNGVEYHYVTITLDLQQVFQIAYVIVKAANSPRPGNWILERSLDDVEYKPWQYHAVTDTECLTLYNIYPRTGPPSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDPSPELLEFTSARYIRLRFQRIRTLNADLMMFAHKDPREIDPIVTRRYYYSVKDISVGGM | ||||||
Domain | 283-339 | Laminin EGF-like 1 | ||||
Sequence: CICYGHARACPLDPATNKSRCECEHNTCGESCDRCCPGFHQKPWRAGTFLTKSECEA | ||||||
Domain | 340-409 | Laminin EGF-like 2 | ||||
Sequence: CNCHGKAEECYYDETVASRNLSLNIHGKYIGGGVCINCTHNTAGINCETCVDGFFRPKGVSPNYPRPCQP | ||||||
Domain | 410-464 | Laminin EGF-like 3 | ||||
Sequence: CHCDPTGSLSEVCVKDEKYAQRGLKPGSCHCKTGFGGVNCDRCVRGYHGYPDCQP | ||||||
Domain | 465-513 | Laminin EGF-like 4 | ||||
Sequence: CNCSGLGSTNEDPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGCEE | ||||||
Domain | 514-523 | Laminin EGF-like 5; first part | ||||
Sequence: CFCSGVSNRC | ||||||
Domain | 527-719 | Laminin IV type A 1 | ||||
Sequence: YWTYGNIQDMRGWYLTDLSGRIRMAPQLDNPDSPQQISISNSEARKSLLDGYYWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTEKILQLMIIFEGNDLRISTAYKEVYLEPSEEHIEEVSLKEEAFTIHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIFRLSSVNLESAVPYPTDRRIATDVEV | ||||||
Domain | 720-752 | Laminin EGF-like 5; second part | ||||
Sequence: CQCPPGYSGSSCETCWPRHRRVNGTIFGGICEP | ||||||
Domain | 753-802 | Laminin EGF-like 6 | ||||
Sequence: CQCFAHAEACDDITGECLNCKDHTGGPYCNECLPGFYGDPTRGSPEDCQP | ||||||
Domain | 803-860 | Laminin EGF-like 7 | ||||
Sequence: CACPLNIPSNNFSPTCHLDRSLGLICDECPIGYTGPRCERCAEGYFGQPSIPGGSCQP | ||||||
Domain | 861-913 | Laminin EGF-like 8 | ||||
Sequence: CQCNDNLDYSIPGSCDSLSGSCLICKPGTTGRYCELCADGYFGDAVNAKNCQP | ||||||
Domain | 914-962 | Laminin EGF-like 9 | ||||
Sequence: CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQLGRGCLP | ||||||
Domain | 963-1009 | Laminin EGF-like 10 | ||||
Sequence: CNCNSFGSKSFDCEASGQCWCQPGVAGKKCDRCAHGYFNFQEGGCIA | ||||||
Domain | 1010-1055 | Laminin EGF-like 11 | ||||
Sequence: CDCSHLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGCKV | ||||||
Domain | 1056-1101 | Laminin EGF-like 12 | ||||
Sequence: CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTL | ||||||
Domain | 1102-1161 | Laminin EGF-like 13 | ||||
Sequence: CDCFLPGTDATTCDLETRKCSCSDQTGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGCSS | ||||||
Domain | 1162-1171 | Laminin EGF-like 14; first part | ||||
Sequence: CYCFGVTSQC | ||||||
Domain | 1172-1375 | Laminin IV type A 2 | ||||
Sequence: SEAKGLIRTWVTLSDEQTILPLVDEALQHTTTKGIAFQKPEIVAKMDEVRQELHLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGTPTHARIITRHMAAPLIGQLTRHEIEMTEKEWKYYGDDPRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGHVLAGSPPAHLIER | ||||||
Domain | 1376-1415 | Laminin EGF-like 14; second part | ||||
Sequence: CDCPPGYSGLSCETCAPGFYRLRSEPGGRTPGPTLGTCVP | ||||||
Domain | 1416-1464 | Laminin EGF-like 15 | ||||
Sequence: CQCNGHSSQCDPETSVCQNCQHHTAGDFCERCALGYYGIVRGLPNDCQP | ||||||
Domain | 1465-1522 | Laminin EGF-like 16 | ||||
Sequence: CACPLISPSNNFSPSCVLEGLEDYRCTACPRGYEGQYCERCAPGYTGSPSSPGGSCQE | ||||||
Domain | 1523-1569 | Laminin EGF-like 17 | ||||
Sequence: CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAECVF | ||||||
Region | 1570-2140 | Domain II and I | ||||
Sequence: CGDECTGLLLGDLARLEQMTMNINLTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSI | ||||||
Coiled coil | 1662-1863 | |||||
Sequence: QDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMS | ||||||
Coiled coil | 1923-2146 | |||||
Sequence: AYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSS | ||||||
Domain | 2141-2324 | Laminin G-like 1 | ||||
Sequence: KVSVSSGGDCVRTYRPEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVRALDGPKASMVPSTYHSVSPPGYTILDVDANAMLFVGGLTGKIKKADAVRVITFTGCMGETYFDNKPIGLWNFREKEGDCKGC | ||||||
Domain | 2336-2517 | Laminin G-like 2 | ||||
Sequence: TIQFDGEGYALVSRPIRWYPNISTVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHNDGKWKAFTLSRIQKQANISIVDIDSNQEENVATSSSGNNFGLDLKADDKIYFGGLPTLRNLSMKARPEVNVKKYSGCLKDIEISRTPYNILSSPDYVGVTKGC | ||||||
Domain | 2522-2706 | Laminin G-like 3 | ||||
Sequence: VYTVSFPKPGFVELAAVSIDVGTEINLSFSTRNESGIILLGSGGTLTPPRRKRRQTTQAYYAIFLNKGRLEVHLSSGTRTMRKIVIKPEPNLFHDGREHSVHVERTRGIFTVQIDEDRRHMQNLTEEQPIEVKKLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINSIPMDFAQPIAFKNADIGRC | ||||||
Domain | 2759-2930 | Laminin G-like 4 | ||||
Sequence: SKQFGLSRNSHIAIAFDDTKVKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDGQWHKIKIVRVKQEGILYVDDASSQTISPKKADILDVVGILYVGGLPINYTTRRIGPVTYSLDGCVRNLHMEQAPVDLDQPTSSFHVGTC | ||||||
Domain | 2929-3115 | Laminin G-like 5 | ||||
Sequence: TCFANAESGTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRPTGVLLGVSSQKMDGMGIEMIDEKLMFHVDNGAGRFTAIYDAGIPGHMCNGQWHKVTAKKIKNRLELVVDGNQVDAQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKLTKGTGKPLEVNFAKALELRGVQPVSC |
Domain
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI, IV and G are globular.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length3,118
- Mass (Da)343,815
- Last updated2013-10-16 v2
- ChecksumCCD31C71B1E0DFD4
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1W2P7N3 | A0A1W2P7N3_MOUSE | Lama2 | 1127 | ||
A0A5F8MPG7 | A0A5F8MPG7_MOUSE | Lama2 | 256 | ||
A0A087WRP2 | A0A087WRP2_MOUSE | Lama2 | 1349 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 616 | in Ref. 1; AAC52165 | ||||
Sequence: I → L | ||||||
Sequence conflict | 646 | in Ref. 1; AAC52165 | ||||
Sequence: I → V | ||||||
Sequence conflict | 678-682 | in Ref. 1; AAC52165 | ||||
Sequence: ERVLM → GEILI | ||||||
Sequence conflict | 704 | in Ref. 1; AAC52165 | ||||
Sequence: A → P | ||||||
Sequence conflict | 853 | in Ref. 1; AAC52165 | ||||
Sequence: I → V | ||||||
Sequence conflict | 908 | in Ref. 1; AAC52165 | ||||
Sequence: A → T | ||||||
Sequence conflict | 917 | in Ref. 1; AAC52165 | ||||
Sequence: N → D | ||||||
Sequence conflict | 925 | in Ref. 1; AAC52165 | ||||
Sequence: I → D | ||||||
Sequence conflict | 1694 | in Ref. 1; AAC52165 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 1840 | in Ref. 1; AAC52165 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 2205 | in Ref. 1; AAC52165 | ||||
Sequence: D → I | ||||||
Sequence conflict | 2214-2215 | in Ref. 1; AAC52165 | ||||
Sequence: EY → GF | ||||||
Sequence conflict | 2523 | in Ref. 1; AAC52165 | ||||
Sequence: Y → N | ||||||
Sequence conflict | 2642 | in Ref. 1; AAC52165 | ||||
Sequence: M → I | ||||||
Sequence conflict | 2729 | in Ref. 1; AAC52165 | ||||
Sequence: P → S | ||||||
Sequence conflict | 2739 | in Ref. 1; AAC52165 | ||||
Sequence: A → V | ||||||
Sequence conflict | 2773 | in Ref. 1; AAC52165 | ||||
Sequence: A → V | ||||||
Sequence conflict | 2802 | in Ref. 1; AAC52165 | ||||
Sequence: A → G | ||||||
Sequence conflict | 2810 | in Ref. 1; AAC52165 | ||||
Sequence: A → G | ||||||
Sequence conflict | 2820 | in Ref. 1; AAC52165 | ||||
Sequence: Y → F | ||||||
Sequence conflict | 2829-2831 | in Ref. 1; AAC52165 | ||||
Sequence: DTS → STR | ||||||
Sequence conflict | 2878 | in Ref. 1; AAC52165 | ||||
Sequence: V → G | ||||||
Sequence conflict | 2946 | in Ref. 1; AAC52165 | ||||
Sequence: A → G | ||||||
Sequence conflict | 2953 | in Ref. 1; AAC52165 | ||||
Sequence: K → I | ||||||
Sequence conflict | 2976 | in Ref. 1; AAC52165 | ||||
Sequence: V → I | ||||||
Sequence conflict | 3011 | in Ref. 1; AAC52165 | ||||
Sequence: G → E | ||||||
Sequence conflict | 3022 | in Ref. 1; AAC52165 | ||||
Sequence: H → Y |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U12147 EMBL· GenBank· DDBJ | AAC52165.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AC101709 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC152982 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC153800 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC155942 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC167232 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC171406 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
X69869 EMBL· GenBank· DDBJ | CAA49502.1 EMBL· GenBank· DDBJ | mRNA | ||
S75315 EMBL· GenBank· DDBJ | AAB33573.1 EMBL· GenBank· DDBJ | mRNA |