Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P53420

- CO4A4_HUMAN

UniProt

P53420 - CO4A4_HUMAN

Protein

Collagen alpha-4(IV) chain

Gene

COL4A4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (22 Sep 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1206 – 12072Cleavage; by collagenaseBy similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. collagen catabolic process Source: Reactome
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. glomerular basement membrane development Source: UniProtKB

    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_16888. Signaling by PDGF.
    REACT_169262. Laminin interactions.
    REACT_18312. NCAM1 interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-4(IV) chain
    Gene namesi
    Name:COL4A4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2206. COL4A4.

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

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Alport syndrome, autosomal recessive (APSAR) [MIM:203780]: A syndrome characterized by progressive glomerulonephritis, glomerular basement membrane defects, renal failure, sensorineural deafness and specific eye abnormalities (lenticonous and macular flecks). The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti441 – 4466Missing in APSAR.
    VAR_008148
    Natural varianti1030 – 10301G → V in APSAR. 1 Publication
    VAR_008153
    Natural varianti1201 – 12011G → S in APSAR. 1 Publication
    VAR_001913
    Natural varianti1572 – 15721P → L in APSAR. 1 Publication
    VAR_008155
    Hematuria, benign familial (BFH) [MIM:141200]: An autosomal dominant condition characterized by non-progressive isolated microscopic hematuria that does not result in renal failure. It is characterized pathologically by thinning of the glomerular basement membrane.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti116 – 1161G → E in BFH. 1 Publication
    VAR_031623
    Natural varianti897 – 8971G → E in BFH. 1 Publication
    VAR_001912
    Natural varianti960 – 9601G → R in BFH. 2 Publications
    VAR_031624
    Natural varianti999 – 9991G → E in BFH. 1 Publication
    Corresponds to variant rs13027659 [ dbSNP | Ensembl ].
    VAR_031625
    Natural varianti1132 – 11321P → L in BFH. 1 Publication
    VAR_031626

    Keywords - Diseasei

    Alport syndrome, Deafness, Disease mutation

    Organism-specific databases

    MIMi141200. phenotype.
    203780. phenotype.
    Orphaneti88918. Autosomal dominant Alport syndrome.
    88919. Autosomal recessive Alport syndrome.
    97562. Benign familial hematuria.
    PharmGKBiPA26721.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 16901652Collagen alpha-4(IV) chainPRO_0000005850Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1480 ↔ 1569Or C-1480 with C-1566PROSITE-ProRule annotation
    Disulfide bondi1513 ↔ 1566Or C-1513 with C-1569PROSITE-ProRule annotation
    Disulfide bondi1525 ↔ 1531PROSITE-ProRule annotation
    Disulfide bondi1588 ↔ 1686Or C-1588 with C-1683PROSITE-ProRule annotation
    Disulfide bondi1622 ↔ 1683Or C-1622 with C-1686PROSITE-ProRule annotation
    Disulfide bondi1634 ↔ 1641PROSITE-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

    PaxDbiP53420.
    PRIDEiP53420.

    PTM databases

    PhosphoSiteiP53420.

    Expressioni

    Tissue specificityi

    Alpha 3 and alpha 4 type IV collagens are colocalized and present in kidney, eye, basement membranes of lens capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers, fetal kidney and fetal lung. PubMed:8083201 reports similar levels of expression of alpha 3 and alpha 4 type IV collagens in kidney, but PubMed:7523402 reports that in kidney levels of alpha 3 type IV collagen are significantly lower than those of alpha 4 type IV collagen. Highest levels of expression of alpha 4 type IV collagen are detected in kidney, calvaria, neuroretina and cardiac muscle. Lower levels of expression are observed in brain, lung and thymus, and no expression is detected in choroid plexus, liver, adrenal, pancreas, ileum or skin.2 Publications

    Gene expression databases

    ArrayExpressiP53420.
    BgeeiP53420.
    CleanExiHS_COL4A4.
    GenevestigatoriP53420.

    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

    BioGridi107683. 1 interaction.
    IntActiP53420. 1 interaction.
    STRINGi9606.ENSP00000379866.

    Structurei

    3D structure databases

    ProteinModelPortaliP53420.
    SMRiP53420. Positions 1465-1688.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1465 – 1690226Collagen IV NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 64267S domainAdd
    BLAST
    Regioni65 – 14591395Triple-helical regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi94 – 963Cell attachment siteSequence Analysis
    Motifi145 – 1473Cell attachment siteSequence Analysis
    Motifi189 – 1913Cell attachment siteSequence Analysis
    Motifi310 – 3123Cell attachment siteSequence Analysis
    Motifi724 – 7263Cell attachment siteSequence Analysis
    Motifi785 – 7873Cell attachment siteSequence Analysis
    Motifi989 – 9913Cell attachment siteSequence Analysis
    Motifi1212 – 12143Cell 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.
    HOGENOMiHOG000085652.
    HOVERGENiHBG004933.
    InParanoidiP53420.
    KOiK06237.
    OMAiPPGYKGF.
    OrthoDBiEOG7RZ5P3.
    PhylomeDBiP53420.
    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. 19 hits.
    [Graphical view]
    SMARTiSM00111. C4. 2 hits.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 2 hits.
    PROSITEiPS51403. NC1_IV. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P53420-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWSLHIVLMR CSFRLTKSLA TGPWSLILIL FSVQYVYGSG KKYIGPCGGR     50
    DCSVCHCVPE KGSRGPPGPP GPQGPIGPLG APGPIGLSGE KGMRGDRGPP 100
    GAAGDKGDKG PTGVPGFPGL DGIPGHPGPP GPRGKPGMSG HNGSRGDPGF 150
    PGGRGALGPG GPLGHPGEKG EKGNSVFILG AVKGIQGDRG DPGLPGLPGS 200
    WGAGGPAGPT GYPGEPGLVG PPGQPGRPGL KGNPGVGVKG QMGDPGEVGQ 250
    QGSPGPTLLV EPPDFCLYKG EKGIKGIPGM VGLPGPPGRK GESGIGAKGE 300
    KGIPGFPGPR GDPGSYGSPG FPGLKGELGL VGDPGLFGLI GPKGDPGNRG 350
    HPGPPGVLVT PPLPLKGPPG DPGFPGRYGE TGDVGPPGPP GLLGRPGEAC 400
    AGMIGPPGPQ GFPGLPGLPG EAGIPGRPDS APGKPGKPGS PGLPGAPGLQ 450
    GLPGSSVIYC SVGNPGPQGI KGKVGPPGGR GPKGEKGNEG LCACEPGPMG 500
    PPGPPGLPGR QGSKGDLGLP GWLGTKGDPG PPGAEGPPGL PGKHGASGPP 550
    GNKGAKGDMV VSRVKGHKGE RGPDGPPGFP GQPGSHGRDG HAGEKGDPGP 600
    PGDHEDATPG GKGFPGPLGP PGKAGPVGPP GLGFPGPPGE RGHPGVPGHP 650
    GVRGPDGLKG QKGDTISCNV TYPGRHGPPG FDGPPGPKGF PGPQGAPGLS 700
    GSDGHKGRPG TPGTAEIPGP PGFRGDMGDP GFGGEKGSSP VGPPGPPGSP 750
    GVNGQKGIPG DPAFGHLGPP GKRGLSGVPG IKGPRGDPGC PGAEGPAGIP 800
    GFLGLKGPKG REGHAGFPGV PGPPGHSCER GAPGIPGQPG LPGYPGSPGA 850
    PGGKGQPGDV GPPGPAGMKG LPGLPGRPGA HGPPGLPGIP GPFGDDGLPG 900
    PPGPKGPRGL PGFPGFPGER GKPGAEGCPG AKGEPGEKGM SGLPGDRGLR 950
    GAKGAIGPPG DEGEMAIISQ KGTPGEPGPP GDDGFPGERG DKGTPGMQGR 1000
    RGEPGRYGPP GFHRGEPGEK GQPGPPGPPG PPGSTGLRGF IGFPGLPGDQ 1050
    GEPGSPGPPG FSGIDGARGP KGNKGDPASH FGPPGPKGEP GSPGCPGHFG 1100
    ASGEQGLPGI QGPRGSPGRP GPPGSSGPPG CPGDHGMPGL RGQPGEMGDP 1150
    GPRGLQGDPG IPGPPGIKGP SGSPGLNGLH GLKGQKGTKG ASGLHDVGPP 1200
    GPVGIPGLKG ERGDPGSPGI SPPGPRGKKG PPGPPGSSGP PGPAGATGRA 1250
    PKDIPDPGPP GDQGPPGPDG PRGAPGPPGL PGSVDLLRGE PGDCGLPGPP 1300
    GPPGPPGPPG YKGFPGCDGK DGQKGPVGFP GPQGPHGFPG PPGEKGLPGP 1350
    PGRKGPTGLP GPRGEPGPPA DVDDCPRIPG LPGAPGMRGP EGAMGLPGMR 1400
    GPSGPGCKGE PGLDGRRGVD GVPGSPGPPG RKGDTGEDGY PGGPGPPGPI 1450
    GDPGPKGFGP GYLGGFLLVL HSQTDQEPTC PLGMPRLWTG YSLLYLEGQE 1500
    KAHNQDLGLA GSCLPVFSTL PFAYCNIHQV CHYAQRNDRS YWLASAAPLP 1550
    MMPLSEEAIR PYVSRCAVCE APAQAVAVHS QDQSIPPCPQ TWRSLWIGYS 1600
    FLMHTGAGDQ GGGQALMSPG SCLEDFRAAP FLECQGRQGT CHFFANKYSF 1650
    WLTTVKADLQ FSSAPAPDTL KESQAQRQKI SRCQVCVKYS 1690
    Length:1,690
    Mass (Da):164,038
    Last modified:September 22, 2009 - v3
    Checksum:iC55711CDF14A57DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1361 – 13633GPR → AIS in AAY24061. (PubMed:15815621)Curated
    Sequence conflicti1659 – 16602LQ → FE in BAA04214. (PubMed:8365481)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61I → T.1 Publication
    Corresponds to variant rs16823264 [ dbSNP | Ensembl ].
    VAR_031622
    Natural varianti116 – 1161G → E in BFH. 1 Publication
    VAR_031623
    Natural varianti441 – 4466Missing in APSAR.
    VAR_008148
    Natural varianti482 – 4821P → S.2 Publications
    Corresponds to variant rs2229814 [ dbSNP | Ensembl ].
    VAR_022069
    Natural varianti545 – 5451G → A.2 Publications
    Corresponds to variant rs1800516 [ dbSNP | Ensembl ].
    VAR_008149
    Natural varianti570 – 5701E → Q.1 Publication
    VAR_008150
    Natural varianti594 – 5941E → G.
    Corresponds to variant rs35998949 [ dbSNP | Ensembl ].
    VAR_055680
    Natural varianti670 – 6701V → I.
    Corresponds to variant rs34236495 [ dbSNP | Ensembl ].
    VAR_055681
    Natural varianti759 – 7591P → L.
    Corresponds to variant rs36121515 [ dbSNP | Ensembl ].
    VAR_055682
    Natural varianti897 – 8971G → E in BFH. 1 Publication
    VAR_001912
    Natural varianti931 – 9311A → T.1 Publication
    Corresponds to variant rs75875272 [ dbSNP | Ensembl ].
    VAR_008151
    Natural varianti960 – 9601G → R in BFH. 2 Publications
    VAR_031624
    Natural varianti999 – 9991G → E in BFH. 1 Publication
    Corresponds to variant rs13027659 [ dbSNP | Ensembl ].
    VAR_031625
    Natural varianti1004 – 10041P → L.2 Publications
    Corresponds to variant rs1800517 [ dbSNP | Ensembl ].
    VAR_008152
    Natural varianti1030 – 10301G → V in APSAR. 1 Publication
    VAR_008153
    Natural varianti1132 – 11321P → L in BFH. 1 Publication
    VAR_031626
    Natural varianti1201 – 12011G → S in APSAR. 1 Publication
    VAR_001913
    Natural varianti1327 – 13271V → M.3 Publications
    Corresponds to variant rs2229813 [ dbSNP | Ensembl ].
    VAR_031627
    Natural varianti1402 – 14021P → S.1 Publication
    VAR_008154
    Natural varianti1403 – 14031S → P.3 Publications
    Corresponds to variant rs3752895 [ dbSNP | Ensembl ].
    VAR_031628
    Natural varianti1572 – 15721P → L in APSAR. 1 Publication
    VAR_008155

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81053 mRNA. Translation: CAA56943.1.
    Y17397
    , Y17398, Y17399, Y17400, Y17401, Y17402, Y17403, Y17404, Y17405, Y17406, Y17407, Y17408, Y17409, Y17410, Y17411, Y17412, Y17413, Y17427, Y17426, Y17414, Y17415, Y17416, Y17417, Y17418, Y17419, Y17420, Y17443, Y17442, Y17441, Y17440, Y17439, Y17438, Y17437, Y17436, Y17435, Y17434, Y17433, Y17432, Y17431, Y17430, Y17429, Y17428, Y17421, Y17422, Y17423, Y17424, Y17425 Genomic DNA. Translation: CAA76763.1.
    AC073149 Genomic DNA. Translation: AAY24061.1.
    AC079235 Genomic DNA. Translation: AAY14670.1.
    AB008496 Genomic DNA. Translation: BAA25065.1.
    D17391 mRNA. Translation: BAA04214.1.
    CCDSiCCDS42828.1.
    PIRiA55360. CGHU1B.
    RefSeqiNP_000083.3. NM_000092.4.
    XP_005246338.1. XM_005246281.1.
    UniGeneiHs.591645.

    Genome annotation databases

    EnsembliENST00000396625; ENSP00000379866; ENSG00000081052.
    GeneIDi1286.
    KEGGihsa:1286.
    UCSCiuc021vxr.1. human.

    Polymorphism databases

    DMDMi259016360.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81053 mRNA. Translation: CAA56943.1 .
    Y17397
    , Y17398 , Y17399 , Y17400 , Y17401 , Y17402 , Y17403 , Y17404 , Y17405 , Y17406 , Y17407 , Y17408 , Y17409 , Y17410 , Y17411 , Y17412 , Y17413 , Y17427 , Y17426 , Y17414 , Y17415 , Y17416 , Y17417 , Y17418 , Y17419 , Y17420 , Y17443 , Y17442 , Y17441 , Y17440 , Y17439 , Y17438 , Y17437 , Y17436 , Y17435 , Y17434 , Y17433 , Y17432 , Y17431 , Y17430 , Y17429 , Y17428 , Y17421 , Y17422 , Y17423 , Y17424 , Y17425 Genomic DNA. Translation: CAA76763.1 .
    AC073149 Genomic DNA. Translation: AAY24061.1 .
    AC079235 Genomic DNA. Translation: AAY14670.1 .
    AB008496 Genomic DNA. Translation: BAA25065.1 .
    D17391 mRNA. Translation: BAA04214.1 .
    CCDSi CCDS42828.1.
    PIRi A55360. CGHU1B.
    RefSeqi NP_000083.3. NM_000092.4.
    XP_005246338.1. XM_005246281.1.
    UniGenei Hs.591645.

    3D structure databases

    ProteinModelPortali P53420.
    SMRi P53420. Positions 1465-1688.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107683. 1 interaction.
    IntActi P53420. 1 interaction.
    STRINGi 9606.ENSP00000379866.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P53420.

    Polymorphism databases

    DMDMi 259016360.

    Proteomic databases

    PaxDbi P53420.
    PRIDEi P53420.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396625 ; ENSP00000379866 ; ENSG00000081052 .
    GeneIDi 1286.
    KEGGi hsa:1286.
    UCSCi uc021vxr.1. human.

    Organism-specific databases

    CTDi 1286.
    GeneCardsi GC02M227867.
    GeneReviewsi COL4A4.
    H-InvDB HIX0030014.
    HGNCi HGNC:2206. COL4A4.
    MIMi 120131. gene.
    141200. phenotype.
    203780. phenotype.
    neXtProti NX_P53420.
    Orphaneti 88918. Autosomal dominant Alport syndrome.
    88919. Autosomal recessive Alport syndrome.
    97562. Benign familial hematuria.
    PharmGKBi PA26721.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085652.
    HOVERGENi HBG004933.
    InParanoidi P53420.
    KOi K06237.
    OMAi PPGYKGF.
    OrthoDBi EOG7RZ5P3.
    PhylomeDBi P53420.
    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_16888. Signaling by PDGF.
    REACT_169262. Laminin interactions.
    REACT_18312. NCAM1 interactions.

    Miscellaneous databases

    ChiTaRSi COL4A4. human.
    GeneWikii COL4A4.
    GenomeRNAii 1286.
    NextBioi 5201.
    PROi P53420.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53420.
    Bgeei P53420.
    CleanExi HS_COL4A4.
    Genevestigatori P53420.

    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. 19 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. "Complete primary structure of the human type IV collagen alpha 4(IV) chain. Comparison with structure and expression of the other alpha (IV) chains."
      Leinonen A., Mariyama M., Mochizuki T., Tryggvason K., Reeders S.T.
      J. Biol. Chem. 269:26172-26177(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS LEU-1004; MET-1327 AND PRO-1403.
      Tissue: Kidney.
    2. "Determination of the genomic structure of the COL4A4 gene and of novel mutations causing autosomal recessive Alport syndrome."
      Boye E., Mollet G., Forestier L., Cohen-Solal L., Heidet L., Cochat P., Gruenfeld J.-P., Palcoux J.-B., Gubler M.-C., Antignac C.
      Am. J. Hum. Genet. 63:1329-1340(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS APSAR VAL-1030 AND LEU-1572, VARIANTS ALA-545; GLN-570; THR-931; LEU-1004; MET-1327; SER-1402 AND PRO-1403.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Two genes, COL4A3 and COL4A4 coding for the human alpha3(IV) and alpha4(IV) collagen chains are arranged head-to-head on chromosome 2q36."
      Momota R., Sugimoto M., Oohashi T., Kigasawa K., Yoshioka H., Ninomiya Y.
      FEBS Lett. 424:11-16(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    5. "cDNA isolation and partial gene structure of the human alpha 4(IV) collagen chain."
      Sugimoto M., Oohashi T., Yoshioka H., Matsuo N., Ninomiya Y.
      FEBS Lett. 330:122-128(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1219-1690, VARIANTS MET-1327 AND PRO-1403.
      Tissue: Eye.
    6. "Isolation and sequencing of cDNAs and genomic DNAs encoding the alpha 4 chain of basement membrane collagen type IV and assignment of the gene to the distal long arm of human chromosome 2."
      Kamagata Y., Mattei M.-G., Ninomiya Y.
      J. Biol. Chem. 267:23753-23758(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1407-1507.
    7. "Complete primary structure of the human alpha 3(IV) collagen chain. Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in human tissues."
      Mariyama M., Leinonen A., Mochizuki T., Tryggvason K., Reeders S.T.
      J. Biol. Chem. 269:23013-23017(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Quaternary organization of the goodpasture autoantigen, the alpha 3(IV) collagen chain. Sequestration of two cryptic autoepitopes by intrapromoter interactions with the alpha4 and alpha5 NC1 domains."
      Borza D.B., Bondar O., Todd P., Sundaramoorthy M., Sado Y., Ninomiya Y., Hudson B.G.
      J. Biol. Chem. 277:40075-40083(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEXAMERIZATION.
    9. Cited for: REVIEW ON VARIANTS.
    10. "Identification of mutations in the alpha 3(IV) and alpha 4(IV) collagen genes in autosomal recessive Alport syndrome."
      Mochizuki T., Lemmink H.H., Mariyama M., Antignac C., Gubler M.-C., Pirson Y., Verellen-Dumoulin C., Chan B., Schroeder C.H., Smeets H.J.M., Reeders S.T.
      Nat. Genet. 8:77-82(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT APSAR SER-1201.
    11. Cited for: VARIANT BFH GLU-897.
    12. "Mutations in the COL4A4 and COL4A3 genes cause familial benign hematuria."
      Badenas C., Praga M., Tazon B., Heidet L., Arrondel C., Armengol A., Andres A., Morales E., Camacho J.A., Lens X., Davila S., Mila M., Antignac C., Darnell A., Torra R.
      J. Am. Soc. Nephrol. 13:1248-1254(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BFH ARG-960, VARIANTS THR-6; SER-482 AND ALA-545.
    13. "Mutations in the COL4A4 gene in thin basement membrane disease."
      Buzza M., Dagher H., Wang Y.Y., Wilson D., Babon J.J., Cotton R.G., Savige J.
      Kidney Int. 63:447-453(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BFH GLU-116; ARG-960; GLU-999 AND LEU-1132, VARIANT SER-482.

    Entry informationi

    Entry nameiCO4A4_HUMAN
    AccessioniPrimary (citable) accession number: P53420
    Secondary accession number(s): A8MTZ1
    , Q53RW9, Q53S42, Q53WR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 154 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 2
      Human chromosome 2: 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