P23229 · ITA6_HUMAN
- ProteinIntegrin alpha-6
- GeneITGA6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1130 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity).
Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome (By similarity).
ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778).
ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760).
ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464).
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 363 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 365 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 367 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 371 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 425 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 427 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 429 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 431 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 433 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 480 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 482 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 484 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 486 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 488 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 634-635 | Cleavage; by PLAU in invasive prostate cancer | ||||
Sequence: RR |
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
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Integrin a6b1 is trafficked specifically by Rab11-FIP5 proteins. The internalization and recycling of a6 integrin by Rab11-FIP5 is specific for the alpha 6 subunit and not observed with a3 integrin or other unrelated type I membrane spanning receptors.
Names & Taxonomy
Protein names
- Recommended nameIntegrin alpha-6
- Alternative names
- Cleaved into 3 chains
- CD Antigen Name
Gene names
- Community suggested namesIntegrin a6b1.
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP23229
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-1050 | Extracellular | ||||
Sequence: FNLDTREDNVIRKYGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQRANRTGGLYSCDITARGPCTRIEFDNDADPTSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETEHDESLVPVPANSYLGLLFLTSVSYTDPDQFVYKTRPPREQPDTFPDVMMNSYLGFSLDSGKGIVSKDEITFVSGAPRANHSGAVVLLKRDMKSAHLLPEHIFDGEGLASSFGYDVAVVDLNKDGWQDIVIGAPQYFDRDGEVGGAVYVYMNQQGRWNNVKPIRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSANGINTKPTQVLKGISPYFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINIQKTITVTPNRIDLRQKTACGAPSGICLQVKSCFEYTANPAGYNPSISIVGTLEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSDEPKTAHIDVHFLKEGCGDDNVCNSNLKLEYKFCTREGNQDKFSYLPIQKGVPELVLKDQKDIALEITVTNSPSNPRNPTKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLTNLGTATLNIQWPKEISNGKWLLYLVKVESKGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQTLNCSVNVNCVNIRCPLRGLDSKASLILRSRLWNSTFLEEYSKLNYLDILMRAFIDVTAAAENIRLPNAGTQVRVTVFPSKTVAQYS | ||||||
Transmembrane | 1051-1076 | Helical | ||||
Sequence: GVPWWIILVAILAGILMLALLVFILW | ||||||
Topological domain | 1077-1130 | Cytoplasmic | ||||
Sequence: KCGFFKRSRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Epidermolysis bullosa, junctional 6, with pyloric atresia (JEB6)
- Note
- DescriptionA form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB6 is an autosomal recessive form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. Clinical manifestations include severe blistering, atrophic scarring, nail dystrophy, and pyloric atresia. Congenital absence of skin (aplasia cutis congenita) is common, and ear anomalies are also relatively common. Disease course is usually severe and often lethal in the neonatal period.
- See alsoMIM:619817
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,228 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue (large scale data), modified residue, lipidation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-23 | UniProt | |||||
Sequence: MAAAGQLCLLYLSAGLLSRLGAA | |||||||
Chain | PRO_0000016259 | 24-938 | UniProt | Integrin alpha-6 heavy chain | |||
Sequence: FNLDTREDNVIRKYGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQRANRTGGLYSCDITARGPCTRIEFDNDADPTSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETEHDESLVPVPANSYLGLLFLTSVSYTDPDQFVYKTRPPREQPDTFPDVMMNSYLGFSLDSGKGIVSKDEITFVSGAPRANHSGAVVLLKRDMKSAHLLPEHIFDGEGLASSFGYDVAVVDLNKDGWQDIVIGAPQYFDRDGEVGGAVYVYMNQQGRWNNVKPIRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSANGINTKPTQVLKGISPYFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINIQKTITVTPNRIDLRQKTACGAPSGICLQVKSCFEYTANPAGYNPSISIVGTLEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSDEPKTAHIDVHFLKEGCGDDNVCNSNLKLEYKFCTREGNQDKFSYLPIQKGVPELVLKDQKDIALEITVTNSPSNPRNPTKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLTNLGTATLNIQWPKEISNGKWLLYLVKVESKGLEKVTCEPQKEINSLNLTESHNSR | |||||||
Chain | PRO_0000016258 | 24-1130 | UniProt | Integrin alpha-6 | |||
Sequence: FNLDTREDNVIRKYGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQRANRTGGLYSCDITARGPCTRIEFDNDADPTSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETEHDESLVPVPANSYLGLLFLTSVSYTDPDQFVYKTRPPREQPDTFPDVMMNSYLGFSLDSGKGIVSKDEITFVSGAPRANHSGAVVLLKRDMKSAHLLPEHIFDGEGLASSFGYDVAVVDLNKDGWQDIVIGAPQYFDRDGEVGGAVYVYMNQQGRWNNVKPIRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSANGINTKPTQVLKGISPYFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINIQKTITVTPNRIDLRQKTACGAPSGICLQVKSCFEYTANPAGYNPSISIVGTLEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSDEPKTAHIDVHFLKEGCGDDNVCNSNLKLEYKFCTREGNQDKFSYLPIQKGVPELVLKDQKDIALEITVTNSPSNPRNPTKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLTNLGTATLNIQWPKEISNGKWLLYLVKVESKGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQTLNCSVNVNCVNIRCPLRGLDSKASLILRSRLWNSTFLEEYSKLNYLDILMRAFIDVTAAAENIRLPNAGTQVRVTVFPSKTVAQYSGVPWWIILVAILAGILMLALLVFILWKCGFFKRSRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS | |||||||
Glycosylation | 78 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 86↔94 | UniProt | |||||
Sequence: CDITARGPC | |||||||
Disulfide bond | 131↔154 | UniProt | |||||
Sequence: CAHRYEKRQHVNTKQESRDIFGRC | |||||||
Disulfide bond | 175↔188 | UniProt | |||||
Sequence: CDGRLRGHEKFGSC | |||||||
Glycosylation | 223 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 323 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 409 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 528↔535 | UniProt | |||||
Sequence: CGAPSGIC | |||||||
Disulfide bond | 541↔601 | UniProt | |||||
Sequence: CFEYTANPAGYNPSISIVGTLEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLKRQKQKVC | |||||||
Chain | PRO_0000425742 | 636-1130 | UniProt | Processed integrin alpha-6 | |||
Sequence: VNSLPEVLPILNSDEPKTAHIDVHFLKEGCGDDNVCNSNLKLEYKFCTREGNQDKFSYLPIQKGVPELVLKDQKDIALEITVTNSPSNPRNPTKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLTNLGTATLNIQWPKEISNGKWLLYLVKVESKGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQTLNCSVNVNCVNIRCPLRGLDSKASLILRSRLWNSTFLEEYSKLNYLDILMRAFIDVTAAAENIRLPNAGTQVRVTVFPSKTVAQYSGVPWWIILVAILAGILMLALLVFILWKCGFFKRSRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS | |||||||
Modified residue (large scale data) | 638 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 665↔671 | UniProt | |||||
Sequence: CGDDNVC | |||||||
Disulfide bond | 765↔776 | UniProt | |||||
Sequence: CVANQNGSQADC | |||||||
Glycosylation | 770 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 787 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 920↔967 | UniProt | Interchain (between heavy and light chains) | ||||
Sequence: CEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQTLNC | |||||||
Glycosylation | 930 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Chain | PRO_0000016260 | 942-1130 | UniProt | Integrin alpha-6 light chain | |||
Sequence: EITEKQIDDNRKFSLFAERKYQTLNCSVNVNCVNIRCPLRGLDSKASLILRSRLWNSTFLEEYSKLNYLDILMRAFIDVTAAAENIRLPNAGTQVRVTVFPSKTVAQYSGVPWWIILVAILAGILMLALLVFILWKCGFFKRSRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS | |||||||
Glycosylation | 966 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 973↔978 | UniProt | |||||
Sequence: CVNIRC | |||||||
Glycosylation | 997 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 1059 | UniProt | In isoform P23229-4; Phosphoserine | ||||
Sequence: V | |||||||
Modified residue | 1064 | UniProt | In isoform P23229-2; Phosphoserine | ||||
Sequence: G | |||||||
Lipidation | 1078 | UniProt | S-palmitoyl cysteine; by DHHC3 | ||||
Sequence: C | |||||||
Modified residue | 1103 | UniProt | In isoform P23229-6; Phosphoserine | ||||
Sequence: R |
Post-translational modification
Production of alpha6p enhances prostate cancer cell invasion and migration (PubMed:17303120).
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Alpha-6 associates with either beta-1 (ITGB1) or beta-4 (ITGB4) to form ITGA6:ITGB1 and ITGA6:ITGB4, respectively (By similarity).
ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion (By similarity).
ITGA6:ITGB4 is found in a ternary complex with NRG1 and ERBB3 (PubMed:20682778).
ITGA6:ITGB4 is found in a ternary complex with IGF1 and IGF1R (PubMed:22351760).
ITGA6:ITGB4 interacts with IGF2 (PubMed:28873464).
Interacts with ADAM9 (By similarity).
Interacts with RAB21 (PubMed:16754960).
Interacts with MDK (PubMed:15466886).
ITGA6:ITGB1 interacts with MDK; this interaction mediates MDK-induced neurite outgrowth (PubMed:15466886).
Interacts with CD82; this interaction down-regulates ITGA6-mediated cell adhesion (PubMed:15557282).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P23229 | CD151 P48509 | 5 | EBI-2436548, EBI-10210332 | |
BINARY | P23229 | ITGB1 P05556 | 2 | EBI-2436548, EBI-703066 | |
BINARY | P23229 | ITGB4 P16144 | 6 | EBI-2436548, EBI-948678 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 30-95 | FG-GAP 1 | ||||
Sequence: EDNVIRKYGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQRANRTGGLYSCDITARGPCT | ||||||
Repeat | 101-166 | FG-GAP 2 | ||||
Sequence: NDADPTSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDD | ||||||
Repeat | 176-229 | FG-GAP 3 | ||||
Sequence: DGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDM | ||||||
Repeat | 283-339 | FG-GAP 4 | ||||
Sequence: EQPDTFPDVMMNSYLGFSLDSGKGIVSKDEITFVSGAPRANHSGAVVLLKRDMKSAH | ||||||
Repeat | 340-402 | FG-GAP 5 | ||||
Sequence: LLPEHIFDGEGLASSFGYDVAVVDLNKDGWQDIVIGAPQYFDRDGEVGGAVYVYMNQQGRWNN | ||||||
Repeat | 403-458 | FG-GAP 6 | ||||
Sequence: VKPIRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSANGINT | ||||||
Repeat | 459-518 | FG-GAP 7 | ||||
Sequence: KPTQVLKGISPYFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINIQKTITVTPN | ||||||
Region | 1077-1083 | Interaction with HPS5 | ||||
Sequence: KCGFFKR | ||||||
Motif | 1079-1083 | GFFKR motif | ||||
Sequence: GFFKR |
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 8 isoforms produced by Alternative splicing. Additional isoforms seem to exist. There is a combination of at least four alternatively spliced domains, two extracellular (X1 and X2) and two cytoplasmic (A and B). So far detected are isoform Alpha-6X1A, isoform Alpha-6X1B and isoform Alpha-6X1X2A (minor). Experimental confirmation may be lacking for some isoforms.
P23229-1
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.
- NameAlpha-6X1X2B
- Length1,130
- Mass (Da)126,606
- Last updated2013-06-26 v5
- ChecksumB53712888B7FE3B6
P23229-2
- NameAlpha-6X1A
- Differences from canonical
- 259-297: Missing
- 1084-1130: SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS → NKKDHYDATYHKAEIHAQPSDKERLTSDA
P23229-3
- NameAlpha-6X1B
- Differences from canonical
- 259-297: Missing
P23229-4
- NameAlpha-6X2A
- Differences from canonical
- 215-258: Missing
- 1084-1130: SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS → NKKDHYDATYHKAEIHAQPSDKERLTSDA
P23229-5
- NameAlpha-6X2B
- Differences from canonical
- 215-258: Missing
P23229-6
- NameAlpha-6X1X2A
- Differences from canonical
- 1084-1130: SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS → NKKDHYDATYHKAEIHAQPSDKERLTSDA
P23229-7
- Name7
- Differences from canonical
- 1-114: Missing
- 215-258: Missing
- 1084-1130: SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS → NKKDHYDATYHKAEIHAQPSDKERLTSDA
P23229-9
- Name9
- Differences from canonical
- 918-932: Missing
- 1084-1130: SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS → NKKDHYDATYHKAEIHAQPSDKERLTSDA
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAQ5BID9 | A0AAQ5BID9_HUMAN | ITGA6 | 977 | ||
C9JXX7 | C9JXX7_HUMAN | ITGA6 | 231 | ||
A0A8C8KBL6 | A0A8C8KBL6_HUMAN | ITGA6 | 1058 | ||
H7BZ97 | H7BZ97_HUMAN | ITGA6 | 258 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_036406 | 1-114 | in isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 69 | in Ref. 1; CAA37655 and 8; CAA42099 | ||||
Sequence: A → G | ||||||
Alternative sequence | VSP_002723 | 215-258 | in isoform Alpha-6X2A, isoform Alpha-6X2B and isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002724 | 259-297 | in isoform Alpha-6X1A and isoform Alpha-6X1B | |||
Sequence: Missing | ||||||
Sequence conflict | 419 | in Ref. 4; BAG59130 and 7; AAI36456/AAI36457 | ||||
Sequence: A → T | ||||||
Sequence conflict | 501 | in Ref. 8; CAA42099 | ||||
Sequence: F → L | ||||||
Sequence conflict | 805 | in Ref. 1; CAA37655 and 3; AAD48469 | ||||
Sequence: D → Y | ||||||
Alternative sequence | VSP_036407 | 918-932 | in isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002725 | 1084-1130 | in isoform Alpha-6X1A, isoform Alpha-6X2A, isoform Alpha-6X1X2A, isoform 7 and isoform 9 | |||
Sequence: SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS → NKKDHYDATYHKAEIHAQPSDKERLTSDA | ||||||
Sequence conflict | 1125 | in Ref. 1; AAB20355 | ||||
Sequence: E → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X53586 EMBL· GenBank· DDBJ | CAA37655.1 EMBL· GenBank· DDBJ | mRNA | ||
AF166343 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166335 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166336 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166337 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166338 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166339 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166340 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166341 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF166342 EMBL· GenBank· DDBJ | AAD48469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK294436 EMBL· GenBank· DDBJ | BAG57680.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK296496 EMBL· GenBank· DDBJ | BAG59130.1 EMBL· GenBank· DDBJ | mRNA | ||
AC078883 EMBL· GenBank· DDBJ | AAX93133.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11177.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC050585 EMBL· GenBank· DDBJ | AAH50585.1 EMBL· GenBank· DDBJ | mRNA | ||
BC136455 EMBL· GenBank· DDBJ | AAI36456.1 EMBL· GenBank· DDBJ | mRNA | ||
BC136456 EMBL· GenBank· DDBJ | AAI36457.1 EMBL· GenBank· DDBJ | mRNA | ||
X59512 EMBL· GenBank· DDBJ | CAA42099.1 EMBL· GenBank· DDBJ | mRNA | ||
S66213 EMBL· GenBank· DDBJ | AAB20355.1 EMBL· GenBank· DDBJ | mRNA | ||
S66196 EMBL· GenBank· DDBJ | AAB20354.1 EMBL· GenBank· DDBJ | mRNA | ||
S52135 EMBL· GenBank· DDBJ | AAB24829.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L40385 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AB208842 EMBL· GenBank· DDBJ | BAD92079.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ858220 EMBL· GenBank· DDBJ | ABH11650.1 EMBL· GenBank· DDBJ | mRNA |