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Q14031

- CO4A6_HUMAN

UniProt

Q14031 - CO4A6_HUMAN

Protein

Collagen alpha-6(IV) chain

Gene

COL4A6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cellular response to amino acid stimulus Source: Ensembl
    3. collagen catabolic process Source: Reactome
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_118779. Extracellular matrix organization.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_150401. Collagen degradation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-6(IV) chain
    Gene namesi
    Name:COL4A6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2208. COL4A6.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen type IV trimer Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Deletions covering the N-terminal regions of COL4A5 and COL4A6, which are localized in a head-to-head manner, are found in the chromosome Xq22.3 centromeric deletion syndrome. This results in a phenotype with features of diffuse leiomyomatosis and Alport syndrome (DL-ATS).
    Deafness, X-linked, 6 (DFNX6) [MIM:300914]: A non-syndromic form of sensorineural hearing loss with prelingual onset. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti591 – 5911G → S in DFNX6. 1 Publication
    VAR_070936

    Keywords - Diseasei

    Deafness, Disease mutation, Non-syndromic deafness

    Organism-specific databases

    MIMi300914. phenotype.
    Orphaneti1018. X-linked diffuse leiomyomatosis - Alport syndrome.
    90625. X-linked nonsyndromic sensorineural deafness type DFN.
    PharmGKBiPA26723.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 16911669Collagen alpha-6(IV) chainPRO_0000005853Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1482 ↔ 1571Or C-1482 with C-1568PROSITE-ProRule annotation
    Disulfide bondi1515 ↔ 1568Or C-1515 with C-1571PROSITE-ProRule annotation
    Disulfide bondi1527 ↔ 1533PROSITE-ProRule annotation
    Disulfide bondi1590 ↔ 1687Or C-1590 with C-1684PROSITE-ProRule annotation
    Disulfide bondi1624 ↔ 1684Or C-1624 with C-1687PROSITE-ProRule annotation
    Disulfide bondi1636 ↔ 1643PROSITE-ProRule annotation

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
    Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
    The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiQ14031.
    PaxDbiQ14031.
    PRIDEiQ14031.

    PTM databases

    PhosphoSiteiQ14031.

    Miscellaneous databases

    PMAP-CutDBQ5JYH8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14031.
    BgeeiQ14031.
    GenevestigatoriQ14031.

    Interactioni

    Subunit structurei

    There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

    Protein-protein interaction databases

    BioGridi107685. 2 interactions.
    IntActiQ14031. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14031.
    SMRiQ14031. Positions 1466-1689.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1467 – 1691225Collagen IV NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 46247S domainAdd
    BLAST
    Regioni47 – 14631417Triple-helical regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi515 – 5173Cell attachment siteSequence Analysis
    Motifi560 – 5623Cell attachment siteSequence Analysis
    Motifi986 – 9883Cell attachment siteSequence Analysis

    Domaini

    Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

    Sequence similaritiesi

    Belongs to the type IV collagen family.PROSITE-ProRule annotation
    Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG004933.
    KOiK06237.
    OrthoDBiEOG7RZ5P3.
    PhylomeDBiQ14031.
    TreeFamiTF344135.

    Family and domain databases

    Gene3Di2.170.240.10. 1 hit.
    InterProiIPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR001442. Collagen_VI_NC.
    [Graphical view]
    PfamiPF01413. C4. 2 hits.
    PF01391. Collagen. 22 hits.
    [Graphical view]
    SMARTiSM00111. C4. 2 hits.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 2 hits.
    PROSITEiPS51403. NC1_IV. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q14031-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLINKLWLLL VTLCLTEELA AAGEKSYGKP CGGQDCSGSC QCFPEKGARG     50
    RPGPIGIQGP TGPQGFTGST GLSGLKGERG FPGLLGPYGP KGDKGPMGVP 100
    GFLGINGIPG HPGQPGPRGP PGLDGCNGTQ GAVGFPGPDG YPGLLGPPGL 150
    PGQKGSKGDP VLAPGSFKGM KGDPGLPGLD GITGPQGAPG FPGAVGPAGP 200
    PGLQGPPGPP GPLGPDGNMG LGFQGEKGVK GDVGLPGPAG PPPSTGELEF 250
    MGFPKGKKGS KGEPGPKGFP GISGPPGFPG LGTTGEKGEK GEKGIPGLPG 300
    PRGPMGSEGV QGPPGQQGKK GTLGFPGLNG FQGIEGQKGD IGLPGPDVFI 350
    DIDGAVISGN PGDPGVPGLP GLKGDEGIQG LRGPSGVPGL PALSGVPGAL 400
    GPQGFPGLKG DQGNPGRTTI GAAGLPGRDG LPGPPGPPGP PSPEFETETL 450
    HNKESGFPGL RGEQGPKGNL GLKGIKGDSG FCACDGGVPN TGPPGEPGPP 500
    GPWGLIGLPG LKGARGDRGS GGAQGPAGAP GLVGPLGPSG PKGKKGEPIL 550
    STIQGMPGDR GDSGSQGFRG VIGEPGKDGV PGLPGLPGLP GDGGQGFPGE 600
    KGLPGLPGEK GHPGPPGLPG NGLPGLPGPR GLPGDKGKDG LPGQQGLPGS 650
    KGITLPCIIP GSYGPSGFPG TPGFPGPKGS RGLPGTPGQP GSSGSKGEPG 700
    SPGLVHLPEL PGFPGPRGEK GLPGFPGLPG KDGLPGMIGS PGLPGSKGAT 750
    GDIFGAENGA PGEQGLQGLT GHKGFLGDSG LPGLKGVHGK PGLLGPKGER 800
    GSPGTPGQVG QPGTPGSSGP YGIKGKSGLP GAPGFPGISG HPGKKGTRGK 850
    KGPPGSIVKK GLPGLKGLPG NPGLVGLKGS PGSPGVAGLP ALSGPKGEKG 900
    SVGFVGFPGI PGLPGIPGTR GLKGIPGSTG KMGPSGRAGT PGEKGDRGNP 950
    GPVGIPSPRR PMSNLWLKGD KGSQGSAGSN GFPGPRGDKG EAGRPGPPGL 1000
    PGAPGLPGII KGVSGKPGPP GFMGIRGLPG LKGSSGITGF PGMPGESGSQ 1050
    GIRGSPGLPG ASGLPGLKGD NGQTVEISGS PGPKGQPGES GFKGTKGRDG 1100
    LIGNIGFPGN KGEDGKVGVS GDVGLPGAPG FPGVAGMRGE PGLPGSSGHQ 1150
    GAIGPLGSPG LIGPKGFPGF PGLHGLNGLP GTKGTHGTPG PSITGVPGPA 1200
    GLPGPKGEKG YPGIGIGAPG KPGLRGQKGD RGFPGLQGPA GLPGAPGISL 1250
    PSLIAGQPGD PGRPGLDGER GRPGPAGPPG PPGPSSNQGD TGDPGFPGIP 1300
    GPKGPKGDQG IPGFSGLPGE LGLKGMRGEP GFMGTPGKVG PPGDPGFPGM 1350
    KGKAGPRGSS GLQGDPGQTP TAEAVQVPPG PLGLPGIDGI PGLTGDPGAQ 1400
    GPVGLQGSKG LPGIPGKDGP SGLPGPPGAL GDPGLPGLQG PPGFEGAPGQ 1450
    QGPFGMPGMP GQSMRVGYTL VKHSQSEQVP PCPIGMSQLW VGYSLLFVEG 1500
    QEKAHNQDLG FAGSCLPRFS TMPFIYCNIN EVCHYARRND KSYWLSTTAP 1550
    IPMMPVSQTQ IPQYISRCSV CEAPSQAIAV HSQDITIPQC PLGWRSLWIG 1600
    YSFLMHTAAG AEGGGQSLVS PGSCLEDFRA TPFIECSGAR GTCHYFANKY 1650
    SFWLTTVEER QQFGELPVSE TLKAGQLHTR VSRCQVCMKS L 1691
    Length:1,691
    Mass (Da):163,807
    Last modified:October 17, 2006 - v3
    Checksum:i9313294D4CE63067
    GO
    Isoform B (identifier: Q14031-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MLINK → MHPG

    Show »
    Length:1,690
    Mass (Da):163,629
    Checksum:iA311225C5FF212B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti170 – 1701M → I in AAA19569. (PubMed:8175748)Curated
    Sequence conflicti170 – 1701M → I in AAA16338. 1 PublicationCurated
    Sequence conflicti272 – 2732IS → LR in AAB19038. (PubMed:8661006)Curated
    Sequence conflicti272 – 2732IS → LR in AAB19039. (PubMed:8661006)Curated
    Sequence conflicti366 – 3661V → D in AAB19038. (PubMed:8661006)Curated
    Sequence conflicti366 – 3661V → D in AAB19039. (PubMed:8661006)Curated
    Sequence conflicti518 – 5181R → Q in AAB19038. (PubMed:8661006)Curated
    Sequence conflicti518 – 5181R → Q in AAB19039. (PubMed:8661006)Curated
    Sequence conflicti917 – 9171P → S in BAA04809. (PubMed:8125972)Curated
    Sequence conflicti917 – 9171P → S in AAB19038. (PubMed:8661006)Curated
    Sequence conflicti917 – 9171P → S in AAB19039. (PubMed:8661006)Curated
    Sequence conflicti1302 – 131312Missing in BAA04809. (PubMed:8125972)CuratedAdd
    BLAST
    Sequence conflicti1356 – 13561P → A in BAA04809. (PubMed:8125972)Curated
    Sequence conflicti1365 – 13651D → H in AAB19038. (PubMed:8661006)Curated
    Sequence conflicti1365 – 13651D → H in AAB19039. (PubMed:8661006)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti455 – 4551S → A.1 Publication
    Corresponds to variant rs1042065 [ dbSNP | Ensembl ].
    VAR_015216
    Natural varianti455 – 4551S → P.
    Corresponds to variant rs1042065 [ dbSNP | Ensembl ].
    VAR_059242
    Natural varianti591 – 5911G → S in DFNX6. 1 Publication
    VAR_070936
    Natural varianti1110 – 11101N → K.1 Publication
    Corresponds to variant rs1042067 [ dbSNP | Ensembl ].
    VAR_015217
    Natural varianti1126 – 11261P → S.
    Corresponds to variant rs35179844 [ dbSNP | Ensembl ].
    VAR_032972
    Natural varianti1130 – 11301G → E in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035748
    Natural varianti1162 – 11621I → V.
    Corresponds to variant rs34466065 [ dbSNP | Ensembl ].
    VAR_032973
    Natural varianti1362 – 13621L → P.
    Corresponds to variant rs35363062 [ dbSNP | Ensembl ].
    VAR_032974

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 55MLINK → MHPG in isoform B. 1 PublicationVSP_001174

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21337 mRNA. Translation: BAA04809.1.
    U04845 mRNA. Translation: AAA19569.2.
    U47004
    , U46959, U46961, U46962, U46963, U46964, U46965, U46966, U46967, U46968, U46969, U46970, U46971, U46972, U46973, U46974, U46975, U46976, U46977, U46978, U46979, U46980, U46981, U46982, U46983, U46984, U46985, U46986, U46987, U46988, U46989, U46990, U46991, U46992, U46993, U46994, U46995, U46996, U46997, U46998, U46999, U47000, U47001, U47002, U47003 Genomic DNA. Translation: AAB19038.1.
    U47004
    , U46960, U46961, U46962, U46963, U46964, U46965, U46966, U46967, U46968, U46969, U46970, U46971, U46972, U46973, U46974, U46975, U46976, U46977, U46978, U46979, U46980, U46981, U46982, U46983, U46984, U46985, U46986, U46987, U46988, U46989, U46990, U46991, U46992, U46993, U46994, U46995, U46996, U46997, U46998, U46999, U47000, U47001, U47002, U47003 Genomic DNA. Translation: AAB19039.1.
    AL136080
    , AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40756.1.
    AL136080
    , AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40758.1.
    AL034369
    , AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42045.1.
    AL034369
    , AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42047.1.
    AL109943
    , AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42993.1.
    AL109943
    , AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42995.1.
    AL031177
    , AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43139.1.
    AL031177
    , AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43140.1.
    CH471120 Genomic DNA. Translation: EAX02688.1.
    L22763 mRNA. Translation: AAA16338.1.
    CCDSiCCDS14541.1. [Q14031-1]
    CCDS14542.1. [Q14031-2]
    PIRiA54122. CGHU6B.
    RefSeqiNP_001274689.1. NM_001287760.1.
    NP_001838.2. NM_001847.3. [Q14031-1]
    NP_378667.1. NM_033641.3. [Q14031-2]
    UniGeneiHs.145586.

    Genome annotation databases

    EnsembliENST00000334504; ENSP00000334733; ENSG00000197565. [Q14031-2]
    ENST00000372216; ENSP00000361290; ENSG00000197565. [Q14031-1]
    GeneIDi1288.
    KEGGihsa:1288.
    UCSCiuc004env.4. human. [Q14031-2]
    uc004enw.4. human. [Q14031-1]

    Polymorphism databases

    DMDMi116241307.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21337 mRNA. Translation: BAA04809.1 .
    U04845 mRNA. Translation: AAA19569.2 .
    U47004
    , U46959 , U46961 , U46962 , U46963 , U46964 , U46965 , U46966 , U46967 , U46968 , U46969 , U46970 , U46971 , U46972 , U46973 , U46974 , U46975 , U46976 , U46977 , U46978 , U46979 , U46980 , U46981 , U46982 , U46983 , U46984 , U46985 , U46986 , U46987 , U46988 , U46989 , U46990 , U46991 , U46992 , U46993 , U46994 , U46995 , U46996 , U46997 , U46998 , U46999 , U47000 , U47001 , U47002 , U47003 Genomic DNA. Translation: AAB19038.1 .
    U47004
    , U46960 , U46961 , U46962 , U46963 , U46964 , U46965 , U46966 , U46967 , U46968 , U46969 , U46970 , U46971 , U46972 , U46973 , U46974 , U46975 , U46976 , U46977 , U46978 , U46979 , U46980 , U46981 , U46982 , U46983 , U46984 , U46985 , U46986 , U46987 , U46988 , U46989 , U46990 , U46991 , U46992 , U46993 , U46994 , U46995 , U46996 , U46997 , U46998 , U46999 , U47000 , U47001 , U47002 , U47003 Genomic DNA. Translation: AAB19039.1 .
    AL136080
    , AL031177 , AL034369 , AL109943 Genomic DNA. Translation: CAI40756.1 .
    AL136080
    , AL031177 , AL034369 , AL109943 Genomic DNA. Translation: CAI40758.1 .
    AL034369
    , AL031177 , AL109943 , AL136080 Genomic DNA. Translation: CAI42045.1 .
    AL034369
    , AL031177 , AL109943 , AL136080 Genomic DNA. Translation: CAI42047.1 .
    AL109943
    , AL031177 , AL034369 , AL136080 Genomic DNA. Translation: CAI42993.1 .
    AL109943
    , AL031177 , AL034369 , AL136080 Genomic DNA. Translation: CAI42995.1 .
    AL031177
    , AL034369 , AL109943 , AL136080 Genomic DNA. Translation: CAI43139.1 .
    AL031177
    , AL034369 , AL109943 , AL136080 Genomic DNA. Translation: CAI43140.1 .
    CH471120 Genomic DNA. Translation: EAX02688.1 .
    L22763 mRNA. Translation: AAA16338.1 .
    CCDSi CCDS14541.1. [Q14031-1 ]
    CCDS14542.1. [Q14031-2 ]
    PIRi A54122. CGHU6B.
    RefSeqi NP_001274689.1. NM_001287760.1.
    NP_001838.2. NM_001847.3. [Q14031-1 ]
    NP_378667.1. NM_033641.3. [Q14031-2 ]
    UniGenei Hs.145586.

    3D structure databases

    ProteinModelPortali Q14031.
    SMRi Q14031. Positions 1466-1689.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107685. 2 interactions.
    IntActi Q14031. 2 interactions.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei Q14031.

    Polymorphism databases

    DMDMi 116241307.

    Proteomic databases

    MaxQBi Q14031.
    PaxDbi Q14031.
    PRIDEi Q14031.

    Protocols and materials databases

    DNASUi 1288.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334504 ; ENSP00000334733 ; ENSG00000197565 . [Q14031-2 ]
    ENST00000372216 ; ENSP00000361290 ; ENSG00000197565 . [Q14031-1 ]
    GeneIDi 1288.
    KEGGi hsa:1288.
    UCSCi uc004env.4. human. [Q14031-2 ]
    uc004enw.4. human. [Q14031-1 ]

    Organism-specific databases

    CTDi 1288.
    GeneCardsi GC0XM107386.
    H-InvDB HIX0056214.
    HGNCi HGNC:2208. COL4A6.
    MIMi 300914. phenotype.
    303631. gene.
    neXtProti NX_Q14031.
    Orphaneti 1018. X-linked diffuse leiomyomatosis - Alport syndrome.
    90625. X-linked nonsyndromic sensorineural deafness type DFN.
    PharmGKBi PA26723.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004933.
    KOi K06237.
    OrthoDBi EOG7RZ5P3.
    PhylomeDBi Q14031.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_118779. Extracellular matrix organization.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_150401. Collagen degradation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.

    Miscellaneous databases

    GeneWikii COL4A6.
    GenomeRNAii 1288.
    NextBioi 5213.
    PMAP-CutDB Q5JYH8.
    PROi Q14031.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14031.
    Bgeei Q14031.
    Genevestigatori Q14031.

    Family and domain databases

    Gene3Di 2.170.240.10. 1 hit.
    InterProi IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR001442. Collagen_VI_NC.
    [Graphical view ]
    Pfami PF01413. C4. 2 hits.
    PF01391. Collagen. 22 hits.
    [Graphical view ]
    SMARTi SM00111. C4. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 2 hits.
    PROSITEi PS51403. NC1_IV. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a new collagen IV chain, alpha 6(IV), by cDNA isolation and assignment of the gene to chromosome Xq22, which is the same locus for COL4A5."
      Oohashi T., Sugimoto M., Mattei M.-G., Ninomiya Y.
      J. Biol. Chem. 269:7520-7526(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
      Tissue: Eye and Kidney.
    2. "Complete primary structure of the sixth chain of human basement membrane collagen, alpha 6(IV). Isolation of the cDNAs for alpha 6(IV) and comparison with five other type IV collagen chains."
      Zhou J., Ding M., Zhao Z., Reeders S.T.
      J. Biol. Chem. 269:13193-13199(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    3. "Structure of the human type IV collagen COL4A6 gene, which is mutated in Alport syndrome-associated leiomyomatosis."
      Zhang X., Zhou J., Reeders S.T., Tryggvason K.
      Genomics 33:473-479(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B), VARIANTS ALA-455 AND LYS-1110.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Deletion of the paired alpha 5(IV) and alpha 6(IV) collagen genes in inherited smooth muscle tumors."
      Zhou J., Mochizuki T., Smeets H., Antignac C., Laurila P., de Paepe A., Tryggvason K., Reeders S.T.
      Science 261:1167-1169(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-542 (ISOFORM A), INVOLVEMENT IN DL-ATS.
    7. Cited for: INVOLVEMENT IN DL-ATS.
    8. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-1130.
    9. "Novel form of X-linked nonsyndromic hearing loss with cochlear malformation caused by a mutation in the type IV collagen gene COL4A6."
      Rost S., Bach E., Neuner C., Nanda I., Dysek S., Bittner R.E., Keller A., Bartsch O., Mlynski R., Haaf T., Mueller C.R., Kunstmann E.
      Eur. J. Hum. Genet. 22:208-215(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DFNX6 SER-591.

    Entry informationi

    Entry nameiCO4A6_HUMAN
    AccessioniPrimary (citable) accession number: Q14031
    Secondary accession number(s): Q12823
    , Q14053, Q5JYH6, Q5JYH8, Q9NQM5, Q9NTX3, Q9UJ76, Q9UMG6, Q9Y4L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3