Q99715 · COCA1_HUMAN
- ProteinCollagen alpha-1(XII) chain
- GeneCOL12A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3063 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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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Aspect | Term | |
---|---|---|
Cellular Component | collagen type XII trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | extracellular vesicle | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Biological Process | cell adhesion | |
Biological Process | collagen fibril organization | |
Biological Process | endodermal cell differentiation |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-1(XII) chain
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99715
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Ullrich congenital muscular dystrophy 2 (UCMD2)
- Note
- DescriptionA form of Ullrich congenital muscular dystrophy, a disease characterized by generalized muscle weakness and striking hypermobility of distal joints in conjunction with variable contractures of more proximal joints and normal intelligence. Additional findings may include kyphoscoliosis, protruded calcanei, and follicular hyperkeratosis (rough skin). More severely affected patients manifest at birth and never achieve independent ambulation, while patients with milder phenotypes might maintain ambulation into adulthood. UCMD2 is a severe, autosomal recessive form with onset at birth.
- See alsoMIM:616470
Bethlem myopathy 2 (BTHLM2)
- Note
- DescriptionA form of Bethlem myopathy, a slowly progressive muscular dystrophy characterized by joint contractures, most frequently affecting the elbows and ankles, and muscle weakness and wasting involving the proximal and extensor muscles more than the distal and flexor ones. The clinical onset more often occurs in childhood or adulthood, but it can be prenatal with decreased fetal movements or neonatal with hypotonia. The hallmark of Bethlem myopathy is long finger flexion contractures. BTHLM2 inheritance is autosomal dominant.
- See alsoMIM:616471
Natural variants in BTHLM2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_074546 | 1965 | R>C | in BTHLM2; uncertain significance; dbSNP:rs200487396 | |
VAR_074547 | 2334 | I>T | in BTHLM2; dbSNP:rs796052093 | |
VAR_074548 | 2786 | G>D | in BTHLM2; dbSNP:rs796052094 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048768 | 461 | in dbSNP:rs34730529 | |||
Sequence: A → P | ||||||
Natural variant | VAR_048769 | 1738 | in dbSNP:rs240736 | |||
Sequence: I → T | ||||||
Natural variant | VAR_074546 | 1965 | in BTHLM2; uncertain significance; dbSNP:rs200487396 | |||
Sequence: R → C | ||||||
Natural variant | VAR_061111 | 2021 | in dbSNP:rs34438461 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_048770 | 2160 | in dbSNP:rs35523808 | |||
Sequence: E → V | ||||||
Natural variant | VAR_074547 | 2334 | in BTHLM2; dbSNP:rs796052093 | |||
Sequence: I → T | ||||||
Natural variant | VAR_048771 | 2596 | in dbSNP:rs35710072 | |||
Sequence: I → V | ||||||
Natural variant | VAR_074548 | 2786 | in BTHLM2; dbSNP:rs796052094 | |||
Sequence: G → D | ||||||
Natural variant | VAR_061112 | 3048 | in dbSNP:rs57396313 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_074549 | 3058 | in dbSNP:rs970547 | |||
Sequence: G → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,611 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-23 | UniProt | |||||
Sequence: MRSRLPPALAALGAALLLSSIEA | |||||||
Chain | PRO_0000005783 | 24-3063 | UniProt | Collagen alpha-1(XII) chain | |||
Sequence: EVDPPSDLNFKIIDENTVHMSWAKPVDPIVGYRITVDPTTDGPTKEFTLSASTTETLLSELVPETEYVVTITSYDEVEESVPVIGQLTIQTGSSTKPVEKKPGKTEIQKCSVSAWTDLVFLVDGSWSVGRNNFKYILDFIAALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYQRDELLAAIKKIPYKGGNTMTGDAIDYLVKNTFTESAGARVGFPKVAIIITDGKSQDEVEIPARELRNVGVEVFSLGIKAADAKELKQIASTPSLNHVFNVANFDAIVDIQNEIISQVCSGVDEQLGELVSGEEVVEPPSNLIAMEVSSKYVKLNWNPSPSPVTGYKVILTPMTAGSRQHALSVGPQTTTLSVRDLSADTEYQISVSAMKGMTSSEPISIMEKTQPMKVQVECSRGVDIKADIVFLVDGSYSIGIANFVKVRAFLEVLVKSFEISPNRVQISLVQYSRDPHTEFTLKKFTKVEDIIEAINTFPYRGGSTNTGKAMTYVREKIFVPSKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVFTVEDFDAFQRISFELTQSICLRIEQELAAIKKKAYVPPKDLSFSEVTSYGFKTNWSPAGENVFSYHITYKEAAGDDEVTVVEPASSTSVVLSSLKPETLYLVNVTAEYEDGFSIPLAGEETTEEVKGAPRNLKVTDETTDSFKITWTQAPGRVLRYRIIYRPVAGGESREVTTPPNQRRRTLENLIPDTKYEVSVIPEYFSGPGTPLTGNAATEEVRGNPRDLRVSDPTTSTMKLSWSGAPGKVKQYLVTYTPVAGGETQEVTVRGDTTNTVLQGLKEGTQYALSVTALYASGAGDALFGEGTTLEERGSPQDLVTKDITDTSIGAYWTSAPGMVRGYRVSWKSLYDDVDTGEKNLPEDAIHTMIENLQPETKYRISVFATYSSGEGEPLTGDATTELSQDSKTLKVDEETENTMRVTWKPAPGKVVNYRVVYRPHGRGKQMVAKVPPTVTSTVLKRLQPQTTYDITVLPIYKMGEGKLRQGSGTTASRFKSPRNLKTSDPTMSSFRVTWEPAPGEVKGYKVTFHPTGDDRRLGELVVGPYDNTVVLEELRAGTTYKVNVFGMFDGGESSPLVGQEMTTLSDTTVMPILSSGMECLTRAEADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTLTGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYNVADFESLSRIVDDLTINLCNSVKGPGDLEAPSNLVISERTHRSFRVSWTPPSDSVDRYKVEYYPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEYSEPLKGTEKTLPVPVVSLNIYDVGPTTMHVQWQPVGGATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVQAVLHDLTSEPVTVREVTLPLPRPQDLKLRDVTHSTMNVFWEPVPGKVRKYIVRYKTPEEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEGESPPVTAQETTRPVPAPTNLKITEVTSEGFRGTWDHGASDVSLYRITWAPFGSSDKMETILNGDENTLVFENLNPNTIYEVSITAIYPDESESDDLIGSERTLPILTTQAPKSGPRNLQVYNATSNSLTVKWDPASGRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDGEGGRMTGRGKTKPLNTVRNLRVYDPSTSTLNVRWDHAEGNPRQYKLFYAPAAGGPEELVPIPGNTNYAILRNLQPDTSYTVTVVPVYTEGDGGRTSDTGRTLMRGLARNVQVYNPTPNSLDVRWDPAPGPVLQYRVVYSPVDGTRPSESIVVPGNTRMVHLERLIPDTLYSVNLVALYSDGEGNPSPAQGRTLPRSGPRNLRVFGETTNSLSVAWDHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDGDGGHLTGNGRTVGLLPPQNIHISDEWYTRFRVSWDPSPSPVLGYKIVYKPVGSNEPMEAFVGEMTSYTLHNLNPSTTYDVNVYAQYDSGLSVPLTDQGTTLYLNVTDLKTYQIGWDTFCVKWSPHRAATSYRLKLSPADGTRGQEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLEGPGVSVKEHTTVKPTEAPTEPPTPPPPPTIPPARDVCKGAKADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDEISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTRTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHVFIVDDFESFEKIEDNLITFVCETATSSCPLIYLDGYTSPGFKMLEAYNLTEKNFASVQGVSLESGSFPSYSAYRIQKNAFVNQPTADLHPNGLPPSYTIILLFRLLPETPSDPFAIWQITDRDYKPQVGVIADPSSKTLSFFNKDTRGEVQTVTFDTEEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAGNITTDGYEILGKLLKGERKSAAFQIQSFDIVCSPVWTSRDRCCDIPSRRDEGKCPAFPNSCTCTQDSVGPPGPPGPAGGPGAKGPRGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLSIPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRGDIASQNMMRAVARQVCEQLISGQMNRFNQMLNQIPNDYQSSRNQPGPPGPPGPPGSAGARGEPGPGGRPGFPGTPGMQGPPGERGLPGEKGERGTGSSGPRGLPGPPGPQGESRTGPPGSTGSRGPPGPPGRPGNSGIRGPPGPPGYCDSSQCASIPYNGQGYPGSG | |||||||
Glycosylation | 329 | UniProt | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 700 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 798 | UniProt | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 889 | UniProt | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 981 | UniProt | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 1763 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2206 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2528 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2679 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 2861 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2864 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2944 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2947 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2950 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2959 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2965 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2968 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2971 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2983 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 3000 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 3003 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 3014 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 3023 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 3026 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 3029 | UniProt | 4-hydroxyproline | ||||
Sequence: P |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for domain, region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-117 | Fibronectin type-III 1 | ||||
Sequence: PPSDLNFKIIDENTVHMSWAKPVDPIVGYRITVDPTTDGPTKEFTLSASTTETLLSELVPETEYVVTITSYDEVEESVPVIGQLTIQTGSS | ||||||
Domain | 140-316 | VWFA 1 | ||||
Sequence: DLVFLVDGSWSVGRNNFKYILDFIAALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYQRDELLAAIKKIPYKGGNTMTGDAIDYLVKNTFTESAGARVGFPKVAIIITDGKSQDEVEIPARELRNVGVEVFSLGIKAADAKELKQIASTPSLNHVFNVANFDAIVDIQNEIISQV | ||||||
Domain | 336-426 | Fibronectin type-III 2 | ||||
Sequence: PPSNLIAMEVSSKYVKLNWNPSPSPVTGYKVILTPMTAGSRQHALSVGPQTTTLSVRDLSADTEYQISVSAMKGMTSSEPISIMEKTQPMK | ||||||
Domain | 440-616 | VWFA 2 | ||||
Sequence: DIVFLVDGSYSIGIANFVKVRAFLEVLVKSFEISPNRVQISLVQYSRDPHTEFTLKKFTKVEDIIEAINTFPYRGGSTNTGKAMTYVREKIFVPSKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVFTVEDFDAFQRISFELTQSI | ||||||
Domain | 634-722 | Fibronectin type-III 3 | ||||
Sequence: PPKDLSFSEVTSYGFKTNWSPAGENVFSYHITYKEAAGDDEVTVVEPASSTSVVLSSLKPETLYLVNVTAEYEDGFSIPLAGEETTEEV | ||||||
Domain | 725-816 | Fibronectin type-III 4 | ||||
Sequence: APRNLKVTDETTDSFKITWTQAPGRVLRYRIIYRPVAGGESREVTTPPNQRRRTLENLIPDTKYEVSVIPEYFSGPGTPLTGNAATEEVRGN | ||||||
Region | 799-830 | Disordered | ||||
Sequence: GPGTPLTGNAATEEVRGNPRDLRVSDPTTSTM | ||||||
Domain | 817-905 | Fibronectin type-III 5 | ||||
Sequence: PRDLRVSDPTTSTMKLSWSGAPGKVKQYLVTYTPVAGGETQEVTVRGDTTNTVLQGLKEGTQYALSVTALYASGAGDALFGEGTTLEER | ||||||
Motif | 862-864 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 907-998 | Fibronectin type-III 6 | ||||
Sequence: SPQDLVTKDITDTSIGAYWTSAPGMVRGYRVSWKSLYDDVDTGEKNLPEDAIHTMIENLQPETKYRISVFATYSSGEGEPLTGDATTELSQD | ||||||
Domain | 999-1087 | Fibronectin type-III 7 | ||||
Sequence: SKTLKVDEETENTMRVTWKPAPGKVVNYRVVYRPHGRGKQMVAKVPPTVTSTVLKRLQPQTTYDITVLPIYKMGEGKLRQGSGTTASRF | ||||||
Region | 1077-1099 | Disordered | ||||
Sequence: RQGSGTTASRFKSPRNLKTSDPT | ||||||
Compositional bias | 1078-1099 | Polar residues | ||||
Sequence: QGSGTTASRFKSPRNLKTSDPT | ||||||
Domain | 1089-1179 | Fibronectin type-III 8 | ||||
Sequence: SPRNLKTSDPTMSSFRVTWEPAPGEVKGYKVTFHPTGDDRRLGELVVGPYDNTVVLEELRAGTTYKVNVFGMFDGGESSPLVGQEMTTLSD | ||||||
Domain | 1199-1371 | VWFA 3 | ||||
Sequence: DIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTLTGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYNVADFESLSRIVDDL | ||||||
Domain | 1387-1476 | Fibronectin type-III 9 | ||||
Sequence: APSNLVISERTHRSFRVSWTPPSDSVDRYKVEYYPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEYSEPLKGTEKTLPVP | ||||||
Domain | 1477-1567 | Fibronectin type-III 10 | ||||
Sequence: VVSLNIYDVGPTTMHVQWQPVGGATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVQAVLHDLTSEPVTVREVTLPLP | ||||||
Domain | 1568-1658 | Fibronectin type-III 11 | ||||
Sequence: RPQDLKLRDVTHSTMNVFWEPVPGKVRKYIVRYKTPEEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEGESPPVTAQETTRPVPAP | ||||||
Domain | 1659-1754 | Fibronectin type-III 12 | ||||
Sequence: TNLKITEVTSEGFRGTWDHGASDVSLYRITWAPFGSSDKMETILNGDENTLVFENLNPNTIYEVSITAIYPDESESDDLIGSERTLPILTTQAPKS | ||||||
Domain | 1755-1849 | Fibronectin type-III 13 | ||||
Sequence: GPRNLQVYNATSNSLTVKWDPASGRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDGEGGRMTGRGKTKPLNTVRN | ||||||
Domain | 1850-1935 | Fibronectin type-III 14 | ||||
Sequence: LRVYDPSTSTLNVRWDHAEGNPRQYKLFYAPAAGGPEELVPIPGNTNYAILRNLQPDTSYTVTVVPVYTEGDGGRTSDTGRTLMRG | ||||||
Domain | 1936-2026 | Fibronectin type-III 15 | ||||
Sequence: LARNVQVYNPTPNSLDVRWDPAPGPVLQYRVVYSPVDGTRPSESIVVPGNTRMVHLERLIPDTLYSVNLVALYSDGEGNPSPAQGRTLPRS | ||||||
Domain | 2027-2117 | Fibronectin type-III 16 | ||||
Sequence: GPRNLRVFGETTNSLSVAWDHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDGDGGHLTGNGRTVGLL | ||||||
Domain | 2118-2206 | Fibronectin type-III 17 | ||||
Sequence: PPQNIHISDEWYTRFRVSWDPSPSPVLGYKIVYKPVGSNEPMEAFVGEMTSYTLHNLNPSTTYDVNVYAQYDSGLSVPLTDQGTTLYLN | ||||||
Domain | 2207-2294 | Fibronectin type-III 18 | ||||
Sequence: VTDLKTYQIGWDTFCVKWSPHRAATSYRLKLSPADGTRGQEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLEGPGVSVKEHTTVKP | ||||||
Region | 2283-2312 | Disordered | ||||
Sequence: GVSVKEHTTVKPTEAPTEPPTPPPPPTIPP | ||||||
Compositional bias | 2297-2312 | Pro residues | ||||
Sequence: APTEPPTPPPPPTIPP | ||||||
Domain | 2323-2496 | VWFA 4 | ||||
Sequence: DIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDEISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTRTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHVFIVDDFESFEKIEDNL | ||||||
Region | 2451-2746 | Nonhelical region (NC3) | ||||
Sequence: SGFSVFVVGVADVDYNELANIASKPSERHVFIVDDFESFEKIEDNLITFVCETATSSCPLIYLDGYTSPGFKMLEAYNLTEKNFASVQGVSLESGSFPSYSAYRIQKNAFVNQPTADLHPNGLPPSYTIILLFRLLPETPSDPFAIWQITDRDYKPQVGVIADPSSKTLSFFNKDTRGEVQTVTFDTEEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAGNITTDGYEILGKLLKGERKSAAFQIQSFDIVCSPVWTSRDRCCDIPSRRDEGKCPAFPNSCTCTQDSV | ||||||
Domain | 2520-2712 | Laminin G-like | ||||
Sequence: GFKMLEAYNLTEKNFASVQGVSLESGSFPSYSAYRIQKNAFVNQPTADLHPNGLPPSYTIILLFRLLPETPSDPFAIWQITDRDYKPQVGVIADPSSKTLSFFNKDTRGEVQTVTFDTEEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAGNITTDGYEILGKLLKGERKSAAFQIQSFDIVCSP | ||||||
Region | 2743-2896 | Disordered | ||||
Sequence: QDSVGPPGPPGPAGGPGAKGPRGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLSIPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRG | ||||||
Domain | 2747-2798 | Collagen-like 1 | ||||
Sequence: GPPGPPGPAGGPGAKGPRGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNG | ||||||
Region | 2747-2898 | Triple-helical region (COL2) with 1 imperfection | ||||
Sequence: GPPGPPGPAGGPGAKGPRGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLSIPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRGDI | ||||||
Compositional bias | 2778-2797 | Pro residues | ||||
Sequence: PRGDIGPPGPQGPPGPQGPN | ||||||
Motif | 2779-2781 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 2802-2852 | Collagen-like 2 | ||||
Sequence: PGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFTGKDGAMGP | ||||||
Compositional bias | 2824-2838 | Pro residues | ||||
Sequence: GTPGLPGPPGPMGPP | ||||||
Domain | 2853-2898 | Collagen-like 3 | ||||
Sequence: RGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRGDI | ||||||
Motif | 2895-2897 | Cell attachment site | ||||
Sequence: RGD | ||||||
Region | 2899-2941 | Nonhelical region (NC2) | ||||
Sequence: ASQNMMRAVARQVCEQLISGQMNRFNQMLNQIPNDYQSSRNQP | ||||||
Region | 2932-3063 | Disordered | ||||
Sequence: NDYQSSRNQPGPPGPPGPPGSAGARGEPGPGGRPGFPGTPGMQGPPGERGLPGEKGERGTGSSGPRGLPGPPGPQGESRTGPPGSTGSRGPPGPPGRPGNSGIRGPPGPPGYCDSSQCASIPYNGQGYPGSG | ||||||
Compositional bias | 2940-2954 | Pro residues | ||||
Sequence: QPGPPGPPGPPGSAG | ||||||
Domain | 2941-2990 | Collagen-like 4 | ||||
Sequence: PGPPGPPGPPGSAGARGEPGPGGRPGFPGTPGMQGPPGERGLPGEKGERG | ||||||
Region | 2942-3044 | Triple-helical region (COL1) with 2 imperfections | ||||
Sequence: GPPGPPGPPGSAGARGEPGPGGRPGFPGTPGMQGPPGERGLPGEKGERGTGSSGPRGLPGPPGPQGESRTGPPGSTGSRGPPGPPGRPGNSGIRGPPGPPGYC | ||||||
Compositional bias | 3018-3036 | Pro residues | ||||
Sequence: GSRGPPGPPGRPGNSGIRG | ||||||
Region | 3045-3063 | Nonhelical region (NC1) | ||||
Sequence: DSSQCASIPYNGQGYPGSG | ||||||
Compositional bias | 3048-3063 | Polar residues | ||||
Sequence: QCASIPYNGQGYPGSG |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing. The final tissue form of collagen XII may contain homotrimers of either isoform 1 or isoform 2 or any combination of isoform 1 and isoform 2.
Q99715-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsLong
- Length3,063
- Mass (Da)333,147
- Last updated2007-05-01 v2
- ChecksumEA38CAFECE8393D2
Q99715-2
- Name2
- SynonymsShort
- Differences from canonical
- 25-1188: Missing
Q99715-4
- Name4
- Differences from canonical
- 2651-2726: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_001149 | 25-1188 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 47 | in Ref. 1; AAC51244 | ||||
Sequence: K → E | ||||||
Sequence conflict | 441-442 | in Ref. 4; AAC01506 | ||||
Sequence: IV → M | ||||||
Sequence conflict | 581 | in Ref. 4; AAC01506 | ||||
Sequence: R → D | ||||||
Sequence conflict | 689 | in Ref. 4; AAC01506 | ||||
Sequence: S → N | ||||||
Sequence conflict | 743 | in Ref. 4; AAC01506 | ||||
Sequence: W → S | ||||||
Sequence conflict | 749 | in Ref. 4; AAC01506 | ||||
Sequence: R → K | ||||||
Sequence conflict | 753 | in Ref. 1; AAC51244 | ||||
Sequence: Y → C | ||||||
Sequence conflict | 813 | in Ref. 4; AAC01506 | ||||
Sequence: V → G | ||||||
Compositional bias | 1078-1099 | Polar residues | ||||
Sequence: QGSGTTASRFKSPRNLKTSDPT | ||||||
Sequence conflict | 1355 | in Ref. 1; AAC51244 | ||||
Sequence: A → D | ||||||
Sequence conflict | 1690 | in Ref. 1; AAC51244 | ||||
Sequence: A → G | ||||||
Sequence conflict | 1729 | in Ref. 1; AAC51244 | ||||
Sequence: P → A | ||||||
Sequence conflict | 1949-1951 | in Ref. 1; AAC51244 | ||||
Sequence: SLD → RLG | ||||||
Compositional bias | 2297-2312 | Pro residues | ||||
Sequence: APTEPPTPPPPPTIPP | ||||||
Sequence conflict | 2614 | in Ref. 5; AAB23937 | ||||
Sequence: P → S | ||||||
Sequence conflict | 2647-2648 | in Ref. 5; AAB23937 | ||||
Sequence: SF → RK | ||||||
Alternative sequence | VSP_024942 | 2651-2726 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 2778-2797 | Pro residues | ||||
Sequence: PRGDIGPPGPQGPPGPQGPN | ||||||
Compositional bias | 2824-2838 | Pro residues | ||||
Sequence: GTPGLPGPPGPMGPP | ||||||
Sequence conflict | 2848 | in Ref. 1; AAC51244 | ||||
Sequence: G → S | ||||||
Sequence conflict | 2858 | in Ref. 1; AAC51244 | ||||
Sequence: P → R | ||||||
Compositional bias | 2940-2954 | Pro residues | ||||
Sequence: QPGPPGPPGPPGSAG | ||||||
Compositional bias | 3018-3036 | Pro residues | ||||
Sequence: GSRGPPGPPGRPGNSGIRG | ||||||
Sequence conflict | 3035 | in Ref. 1; AAC51244 | ||||
Sequence: R → Q | ||||||
Compositional bias | 3048-3063 | Polar residues | ||||
Sequence: QCASIPYNGQGYPGSG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U73778 EMBL· GenBank· DDBJ | AAC51244.1 EMBL· GenBank· DDBJ | mRNA | ||
U73779 EMBL· GenBank· DDBJ | AAD40483.1 EMBL· GenBank· DDBJ | mRNA | ||
AL080250 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL354664 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL096771 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF061871 EMBL· GenBank· DDBJ | AAC83578.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U68139 EMBL· GenBank· DDBJ | AAC01506.1 EMBL· GenBank· DDBJ | mRNA | ||
AH004088 EMBL· GenBank· DDBJ | AAB23937.2 EMBL· GenBank· DDBJ | Genomic DNA |