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Q29442

- CO4A4_BOVIN

UniProt

Q29442 - CO4A4_BOVIN

Protein

Collagen alpha-4(IV) chain

Gene

COL4A4

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-4(IV) chain
    Gene namesi
    Name:COL4A4
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane PROSITE-ProRule annotation
    Note: Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).By similarity

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. collagen type IV trimer Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 453›453Collagen alpha-4(IV) chainPRO_0000059413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi243 ↔ 332Or C-243 with C-329PROSITE-ProRule annotation
    Disulfide bondi276 ↔ 329Or C-276 with C-332PROSITE-ProRule annotation
    Disulfide bondi288 ↔ 294PROSITE-ProRule annotation
    Disulfide bondi351 ↔ 449Or C-351 with C-446PROSITE-ProRule annotation
    Disulfide bondi385 ↔ 446Or C-385 with C-449PROSITE-ProRule annotation
    Disulfide bondi397 ↔ 404PROSITE-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, Hydroxylation

    Proteomic databases

    PRIDEiQ29442.

    Expressioni

    Tissue specificityi

    Alpha 3 and alpha 4 type IV collagens are colocalized and present only in basement membranes of kidney, eye, cochlea, lung and brain.

    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. The alpha 3(IV) chain forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this triple helical structure dimerizes through NC1-NC1 domain interactions such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV) chains of the opposite protomer, respectively. Associates with LAMB2 at the neuromuscular junction and in GBM By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000018302.

    Structurei

    3D structure databases

    ProteinModelPortaliQ29442.
    SMRiQ29442. Positions 228-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini228 – 453226Collagen IV NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni‹1 – 222›222Triple-helical regionAdd
    BLAST

    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

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000085652.
    HOVERGENiHBG004933.
    InParanoidiQ29442.

    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. 3 hits.
    [Graphical view]
    SMARTiSM00111. C4. 2 hits.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 2 hits.
    PROSITEiPS51403. NC1_IV. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q29442-1 [UniParc]FASTAAdd to Basket

    « Hide

    GPPGPPGAPG KALKGDIPDP GLPGDQGPPG PDGPRGVPGP PGPPGSVDLL    50
    KGEPGDCGLP GPPGLPGPPG PPGHKGFPGC DGKHGQKGPM GFPGPQGPPG 100
    SPGPPGDKGL PGPPGRRGPL GPPGSRGEPG PPADLDACPR IPGLPGVPGP 150
    RGPEGTMGLP GMRGPPGPGC KGEPGLDGRR GEDGLPGSPG PPGHKGDMGE 200
    AGCPGAPGPP GPMGDPGPIG FGPGYLSGFL LVLHSQTDGE PTCPMGMPRL 250
    WTGYSLLYLE GQERAHNQDL GLAGSCLPIF STLPFAYCNI HQVCHYARRN 300
    DRSYWLASTA PLPMTPLSED EIRPYISRCA VCEAPAQAVA VHSQDQSIPP 350
    CPRAWRSLWI GYSFLMHTGA GDQGGGQALM SPGSCLEDFR AAPFLECQGR 400
    QGTCHFFANK YSFWLTTVRP DLQFSSAPLP DTLKESHAQR QKISRCQVCV 450
    KHS 453
    Length:453
    Mass (Da):46,385
    Last modified:November 1, 1997 - v1
    Checksum:iF7ED410AE9A65BC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Sequence conflicti219 – 2191I → P AA sequence (PubMed:1468209)Curated
    Sequence conflicti219 – 2191I → P AA sequence (PubMed:2318822)Curated
    Sequence conflicti219 – 2191I → P AA sequence (PubMed:2438283)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77480 mRNA. Translation: AAA30458.2. Sequence problems.
    PIRiS18804.
    UniGeneiBt.91476.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77480 mRNA. Translation: AAA30458.2 . Sequence problems.
    PIRi S18804.
    UniGenei Bt.91476.

    3D structure databases

    ProteinModelPortali Q29442.
    SMRi Q29442. Positions 228-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000018302.

    Proteomic databases

    PRIDEi Q29442.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085652.
    HOVERGENi HBG004933.
    InParanoidi Q29442.

    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. 3 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. "The alpha 4(IV) chain of basement membrane collagen. Isolation of cDNAs encoding bovine alpha 4(IV) and comparison with other type IV collagens."
      Mariyama M., Kalluri R., Hudson B.G., Reeders S.T.
      J. Biol. Chem. 267:1253-1258(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 317-328.
      Tissue: Lens.
    2. "Partial protein sequence of the globular domain of alpha 4(IV) collagen chain: sites of sequence variability and homology with alpha 2(IV)."
      Matsukura H., Michael A.F., Fish A.J., Butkowski R.J.
      Connect. Tissue Res. 28:231-244(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 217-255; 257-278; 303-314; 391-399 AND 411-434.
    3. "Glomerular basement membrane. Identification of a fourth chain, alpha 4, of type IV collagen."
      Gunwar S., Saus J., Noelken M.E., Hudson B.G.
      J. Biol. Chem. 265:5466-5469(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 217-246.
    4. "Glomerular basement membrane. Identification of dimeric subunits of the noncollagenous domain (hexamer) of collagen IV and the Goodpasture antigen."
      Gunwar S., Ballester F., Kalluri R., Timoneda J., Chonko A.M., Edwards S.J., Noelken M.E., Hudson B.G.
      J. Biol. Chem. 266:15318-15324(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 217-237.
    5. "Localization of the Goodpasture epitope to a novel chain of basement membrane collagen."
      Butkowski R.J., Langeveld J.P.M., Wieslander J., Hamilton J., Hudson B.G.
      J. Biol. Chem. 262:7874-7877(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 217-233.

    Entry informationi

    Entry nameiCO4A4_BOVIN
    AccessioniPrimary (citable) accession number: Q29442
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3