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P02462

- CO4A1_HUMAN

UniProt

P02462 - CO4A1_HUMAN

Protein

Collagen alpha-1(IV) chain

Gene

COL4A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (06 Feb 2007)
      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.
    Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.

    GO - Molecular functioni

    1. extracellular matrix constituent conferring elasticity Source: BHF-UCL
    2. extracellular matrix structural constituent Source: BHF-UCL
    3. platelet-derived growth factor binding Source: MGI
    4. protein binding Source: IntAct

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. basement membrane organization Source: BHF-UCL
    3. blood vessel morphogenesis Source: BHF-UCL
    4. brain development Source: BHF-UCL
    5. cellular response to amino acid stimulus Source: Ensembl
    6. collagen catabolic process Source: Reactome
    7. epithelial cell differentiation Source: Ensembl
    8. extracellular matrix disassembly Source: Reactome
    9. extracellular matrix organization Source: Reactome
    10. neuromuscular junction development Source: Ensembl
    11. patterning of blood vessels Source: BHF-UCL
    12. renal tubule morphogenesis Source: BHF-UCL
    13. retinal blood vessel morphogenesis Source: BHF-UCL

    Keywords - Biological processi

    Angiogenesis

    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_163699. Scavenging by Class A Receptors.
    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-1(IV) chain
    Cleaved into the following chain:
    Gene namesi
    Name:COL4A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:2202. COL4A1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: BHF-UCL
    2. collagen type IV trimer Source: BHF-UCL
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Brain small vessel disease with hemorrhage (BSVDH) [MIM:607595]: An autosomal dominant disease characterized by weakening of the blood vessels in the brain and retinal arteriolar tortuosity. In affected individuals, stroke is often the first symptom and is usually caused by bleeding in the brain (hemorrhagic stroke) rather than a lack of blood flow in the brain (ischemic stroke). Patients also have leukoencephalopathy and may experience seizures and migraine headaches accompanied by visual sensations known as auras.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti562 – 5621G → E in BSVDH. 1 Publication
    VAR_030028
    Natural varianti720 – 7201G → D in BSVDH; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy. 2 Publications
    VAR_064496
    Natural varianti755 – 7551G → R in BSVDH; associated with ocular anomalies of variable severity in some patients. 2 Publications
    VAR_064497
    Natural varianti805 – 8051G → R in BSVDH. 1 Publication
    VAR_064498
    Hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:611773]: The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti498 – 4981G → R in HANAC. 1 Publication
    VAR_064493
    Natural varianti498 – 4981G → V in HANAC. 1 Publication
    VAR_044159
    Natural varianti510 – 5101G → R in HANAC. 1 Publication
    VAR_064494
    Natural varianti519 – 5191G → R in HANAC. 1 Publication
    VAR_044160
    Natural varianti525 – 5251G → L in HANAC; requires 2 nucleotide substitutions. 1 Publication
    VAR_064495
    Natural varianti528 – 5281G → E in HANAC. 1 Publication
    VAR_044161
    Porencephaly 1 (POREN1) [MIM:175780]: A neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres, neurologic manifestations, facial paresis, and visual defects. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti749 – 7491G → S in POREN1. 1 Publication
    VAR_030029
    Natural varianti1130 – 11301G → D in POREN1. 1 Publication
    VAR_030030
    Natural varianti1236 – 12361G → R in POREN1. 1 Publication
    VAR_030031
    Natural varianti1423 – 14231G → R in POREN1. 1 Publication
    VAR_030032
    Natural varianti1580 – 15801G → R in POREN1. 1 Publication
    VAR_064499

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi175780. phenotype.
    607595. phenotype.
    611773. phenotype.
    Orphaneti73229. Autosomal dominant familial hematuria - retinal arteriolar tortuosity - contractures.
    99810. Familial porencephaly.
    36383. Familial vascular leukoencephalopathy.
    799. Schizencephaly.
    899. Walker-Warburg syndrome.
    PharmGKBiPA26717.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Propeptidei28 – 172145N-terminal propeptide (7S domain)PRO_0000005748Add
    BLAST
    Chaini173 – 16691497Collagen alpha-1(IV) chainPRO_0000005749Add
    BLAST
    Chaini1445 – 1669225ArrestenPRO_0000390482Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi126 – 1261N-linked (GlcNAc...)
    Disulfide bondi1460 ↔ 15511 PublicationPROSITE-ProRule annotation
    Disulfide bondi1493 ↔ 15481 PublicationPROSITE-ProRule annotation
    Disulfide bondi1505 ↔ 15111 PublicationPROSITE-ProRule annotation
    Cross-linki1533 – 1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)
    Disulfide bondi1570 ↔ 16651 PublicationPROSITE-ProRule annotation
    Disulfide bondi1604 ↔ 16621 PublicationPROSITE-ProRule annotation
    Disulfide bondi1616 ↔ 16221 PublicationPROSITE-ProRule annotation
    Cross-linki1651 – 1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)

    Post-translational modificationi

    Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.
    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.
    Proteolytic processing produces the C-terminal NC1 peptide, arresten.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiP02462.
    PaxDbiP02462.
    PRIDEiP02462.

    PTM databases

    PhosphoSiteiP02462.

    Expressioni

    Tissue specificityi

    Highly expressed in placenta.2 Publications

    Gene expression databases

    ArrayExpressiP02462.
    BgeeiP02462.
    CleanExiHS_COL4A1.
    GenevestigatoriP02462.

    Organism-specific databases

    HPAiCAB001695.
    HPA054039.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COL4A2P085722EBI-2432478,EBI-2432506

    Protein-protein interaction databases

    BioGridi107679. 14 interactions.
    IntActiP02462. 24 interactions.
    MINTiMINT-6743187.
    STRINGi9606.ENSP00000364979.

    Structurei

    Secondary structure

    1
    1669
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1446 – 14516
    Beta strandi1453 – 14564
    Beta strandi1465 – 147814
    Beta strandi1481 – 14844
    Helixi1490 – 14923
    Beta strandi1493 – 14964
    Beta strandi1502 – 15054
    Beta strandi1509 – 15146
    Beta strandi1519 – 15246
    Helixi1538 – 15447
    Beta strandi1547 – 15559
    Beta strandi1557 – 15615
    Beta strandi1563 – 15664
    Beta strandi1574 – 158714
    Helixi1589 – 15913
    Beta strandi1593 – 15953
    Helixi1601 – 16033
    Beta strandi1604 – 16074
    Beta strandi1613 – 16175
    Beta strandi1620 – 16234
    Beta strandi1629 – 16346
    Helixi1638 – 16403
    Beta strandi1648 – 16514
    Helixi1655 – 16584
    Beta strandi1661 – 16677

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LI1X-ray1.90A/B/D/E1441-1669[»]
    ProteinModelPortaliP02462.
    SMRiP02462. Positions 1442-1669.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02462.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1445 – 1669225Collagen IV NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 14401268Triple-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, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG004933.
    KOiK06237.
    OMAiSSMDHGF.
    OrthoDBiEOG7RZ5P3.
    PhylomeDBiP02462.
    TreeFamiTF316865.

    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. 21 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 1 (identifier: P02462-1) [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

    MGPRLSVWLL LLPAALLLHE EHSRAAAKGG CAGSGCGKCD CHGVKGQKGE     50
    RGLPGLQGVI GFPGMQGPEG PQGPPGQKGD TGEPGLPGTK GTRGPPGASG 100
    YPGNPGLPGI PGQDGPPGPP GIPGCNGTKG ERGPLGPPGL PGFAGNPGPP 150
    GLPGMKGDPG EILGHVPGML LKGERGFPGI PGTPGPPGLP GLQGPVGPPG 200
    FTGPPGPPGP PGPPGEKGQM GLSFQGPKGD KGDQGVSGPP GVPGQAQVQE 250
    KGDFATKGEK GQKGEPGFQG MPGVGEKGEP GKPGPRGKPG KDGDKGEKGS 300
    PGFPGEPGYP GLIGRQGPQG EKGEAGPPGP PGIVIGTGPL GEKGERGYPG 350
    TPGPRGEPGP KGFPGLPGQP GPPGLPVPGQ AGAPGFPGER GEKGDRGFPG 400
    TSLPGPSGRD GLPGPPGSPG PPGQPGYTNG IVECQPGPPG DQGPPGIPGQ 450
    PGFIGEIGEK GQKGESCLIC DIDGYRGPPG PQGPPGEIGF PGQPGAKGDR 500
    GLPGRDGVAG VPGPQGTPGL IGQPGAKGEP GEFYFDLRLK GDKGDPGFPG 550
    QPGMTGRAGS PGRDGHPGLP GPKGSPGSVG LKGERGPPGG VGFPGSRGDT 600
    GPPGPPGYGP AGPIGDKGQA GFPGGPGSPG LPGPKGEPGK IVPLPGPPGA 650
    EGLPGSPGFP GPQGDRGFPG TPGRPGLPGE KGAVGQPGIG FPGPPGPKGV 700
    DGLPGDMGPP GTPGRPGFNG LPGNPGVQGQ KGEPGVGLPG LKGLPGLPGI 750
    PGTPGEKGSI GVPGVPGEHG AIGPPGLQGI RGEPGPPGLP GSVGSPGVPG 800
    IGPPGARGPP GGQGPPGLSG PPGIKGEKGF PGFPGLDMPG PKGDKGAQGL 850
    PGITGQSGLP GLPGQQGAPG IPGFPGSKGE MGVMGTPGQP GSPGPVGAPG 900
    LPGEKGDHGF PGSSGPRGDP GLKGDKGDVG LPGKPGSMDK VDMGSMKGQK 950
    GDQGEKGQIG PIGEKGSRGD PGTPGVPGKD GQAGQPGQPG PKGDPGISGT 1000
    PGAPGLPGPK GSVGGMGLPG TPGEKGVPGI PGPQGSPGLP GDKGAKGEKG 1050
    QAGPPGIGIP GLRGEKGDQG IAGFPGSPGE KGEKGSIGIP GMPGSPGLKG 1100
    SPGSVGYPGS PGLPGEKGDK GLPGLDGIPG VKGEAGLPGT PGPTGPAGQK 1150
    GEPGSDGIPG SAGEKGEPGL PGRGFPGFPG AKGDKGSKGE VGFPGLAGSP 1200
    GIPGSKGEQG FMGPPGPQGQ PGLPGSPGHA TEGPKGDRGP QGQPGLPGLP 1250
    GPMGPPGLPG IDGVKGDKGN PGWPGAPGVP GPKGDPGFQG MPGIGGSPGI 1300
    TGSKGDMGPP GVPGFQGPKG LPGLQGIKGD QGDQGVPGAK GLPGPPGPPG 1350
    PYDIIKGEPG LPGPEGPPGL KGLQGLPGPK GQQGVTGLVG IPGPPGIPGF 1400
    DGAPGQKGEM GPAGPTGPRG FPGPPGPDGL PGSMGPPGTP SVDHGFLVTR 1450
    HSQTIDDPQC PSGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM 1500
    PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPITGEN IRPFISRCAV 1550
    CEAPAMVMAV HSQTIQIPPC PSGWSSLWIG YSFVMHTSAG AEGSGQALAS 1600
    PGSCLEEFRS APFIECHGRG TCNYYANAYS FWLATIERSE MFKKPTPSTL 1650
    KAGELRTHVS RCQVCMRRT 1669
    Length:1,669
    Mass (Da):160,615
    Last modified:February 6, 2007 - v3
    Checksum:i3C9BCD8E410A9ED1
    GO
    Isoform 2 (identifier: P02462-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         498-848: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,318
    Mass (Da):127,981
    Checksum:iE313ADCF65DA7BEC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2382SG → KE AA sequence (PubMed:4043082)Curated
    Sequence conflicti241 – 2411G → K AA sequence (PubMed:4043082)Curated
    Sequence conflicti319 – 3191Q → A in CAA29075. (PubMed:3311751)Curated
    Sequence conflicti719 – 7191N → D AA sequence (PubMed:6434307)Curated
    Sequence conflicti837 – 8371D → Y AA sequence (PubMed:6434307)Curated
    Sequence conflicti842 – 8421K → P AA sequence (PubMed:6434307)Curated
    Sequence conflicti896 – 8961V → W in CAA68698. (PubMed:3691802)Curated
    Sequence conflicti904 – 9041E → Q AA sequence (PubMed:6434307)Curated
    Sequence conflicti914 – 9141S → K AA sequence (PubMed:6434307)Curated
    Sequence conflicti998 – 9981S → K AA sequence (PubMed:6434307)Curated
    Sequence conflicti1010 – 10101K → P AA sequence (PubMed:6434307)Curated
    Sequence conflicti1012 – 10121S → K AA sequence (PubMed:6434307)Curated
    Sequence conflicti1358 – 13581E → Q AA sequence (PubMed:6434307)Curated
    Sequence conflicti1490 – 14901A → T in ABE73157. (PubMed:16481288)Curated
    Sequence conflicti1507 – 15071I → T in ABE73157. (PubMed:16481288)Curated
    Sequence conflicti1519 – 15191Y → C in ABE73157. (PubMed:16481288)Curated
    Sequence conflicti1570 – 15701C → Y in AAM97359. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71V → L.1 Publication
    Corresponds to variant rs9515185 [ dbSNP | Ensembl ].
    VAR_030027
    Natural varianti304 – 3041P → L.
    Corresponds to variant rs34843786 [ dbSNP | Ensembl ].
    VAR_044158
    Natural varianti498 – 4981G → R in HANAC. 1 Publication
    VAR_064493
    Natural varianti498 – 4981G → V in HANAC. 1 Publication
    VAR_044159
    Natural varianti510 – 5101G → R in HANAC. 1 Publication
    VAR_064494
    Natural varianti519 – 5191G → R in HANAC. 1 Publication
    VAR_044160
    Natural varianti525 – 5251G → L in HANAC; requires 2 nucleotide substitutions. 1 Publication
    VAR_064495
    Natural varianti528 – 5281G → E in HANAC. 1 Publication
    VAR_044161
    Natural varianti555 – 5551T → P.5 Publications
    Corresponds to variant rs536174 [ dbSNP | Ensembl ].
    VAR_030511
    Natural varianti562 – 5621G → E in BSVDH. 1 Publication
    VAR_030028
    Natural varianti720 – 7201G → D in BSVDH; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy. 2 Publications
    VAR_064496
    Natural varianti749 – 7491G → S in POREN1. 1 Publication
    VAR_030029
    Natural varianti755 – 7551G → R in BSVDH; associated with ocular anomalies of variable severity in some patients. 2 Publications
    VAR_064497
    Natural varianti805 – 8051G → R in BSVDH. 1 Publication
    VAR_064498
    Natural varianti1130 – 11301G → D in POREN1. 1 Publication
    VAR_030030
    Natural varianti1236 – 12361G → R in POREN1. 1 Publication
    VAR_030031
    Natural varianti1334 – 13341Q → H.2 Publications
    Corresponds to variant rs3742207 [ dbSNP | Ensembl ].
    VAR_020013
    Natural varianti1423 – 14231G → R in POREN1. 1 Publication
    VAR_030032
    Natural varianti1580 – 15801G → R in POREN1. 1 Publication
    VAR_064499

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei498 – 848351Missing in isoform 2. CuratedVSP_034644Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26576
    , J04217, M26550, M26540, M26542, M26543, M26544, M26545, M26546, M26547, M26537, M26538, M26548, M26549, M26551, M26552, M26553, M26554, M26555, M26556, M26557, M26539, M26558, M26559, M26560, M26561, M26562, M26536, M26563, M26541, M26564, M26565, M26566, M26567, M26568, M26569, M26570, M26571, M26572, M26573, M26574, M26575 Genomic DNA. Translation: AAA53098.1.
    AL161773, AL390755 Genomic DNA. Translation: CAH71365.1.
    AL390755, AL161773 Genomic DNA. Translation: CAH74130.1.
    AL161773, AL390755 Genomic DNA. Translation: CAM14222.1.
    AL390755, AL161773 Genomic DNA. Translation: CAM20295.1.
    BC047305 mRNA. Translation: AAH47305.1.
    BC151220 mRNA. Translation: AAI51221.1.
    X05561 mRNA. Translation: CAA29075.1.
    Y00706 mRNA. Translation: CAA68698.1.
    M10940 mRNA. Translation: AAA52006.1.
    M11315 mRNA. Translation: AAA52042.1.
    AF258349 mRNA. Translation: AAF72630.1.
    AF363672 mRNA. Translation: AAK53382.1.
    AF400431 mRNA. Translation: AAK92480.1.
    AY285780 mRNA. Translation: AAP43112.1.
    AF536207 mRNA. Translation: AAM97359.1.
    DQ464183 mRNA. Translation: ABE73157.1.
    CCDSiCCDS9511.1. [P02462-1]
    PIRiS16876. CGHU4B.
    RefSeqiNP_001836.2. NM_001845.4. [P02462-1]
    UniGeneiHs.17441.

    Genome annotation databases

    EnsembliENST00000375820; ENSP00000364979; ENSG00000187498. [P02462-1]
    GeneIDi1282.
    KEGGihsa:1282.
    UCSCiuc001vqw.4. human. [P02462-1]

    Polymorphism databases

    DMDMi125987809.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26576
    , J04217 , M26550 , M26540 , M26542 , M26543 , M26544 , M26545 , M26546 , M26547 , M26537 , M26538 , M26548 , M26549 , M26551 , M26552 , M26553 , M26554 , M26555 , M26556 , M26557 , M26539 , M26558 , M26559 , M26560 , M26561 , M26562 , M26536 , M26563 , M26541 , M26564 , M26565 , M26566 , M26567 , M26568 , M26569 , M26570 , M26571 , M26572 , M26573 , M26574 , M26575 Genomic DNA. Translation: AAA53098.1 .
    AL161773 , AL390755 Genomic DNA. Translation: CAH71365.1 .
    AL390755 , AL161773 Genomic DNA. Translation: CAH74130.1 .
    AL161773 , AL390755 Genomic DNA. Translation: CAM14222.1 .
    AL390755 , AL161773 Genomic DNA. Translation: CAM20295.1 .
    BC047305 mRNA. Translation: AAH47305.1 .
    BC151220 mRNA. Translation: AAI51221.1 .
    X05561 mRNA. Translation: CAA29075.1 .
    Y00706 mRNA. Translation: CAA68698.1 .
    M10940 mRNA. Translation: AAA52006.1 .
    M11315 mRNA. Translation: AAA52042.1 .
    AF258349 mRNA. Translation: AAF72630.1 .
    AF363672 mRNA. Translation: AAK53382.1 .
    AF400431 mRNA. Translation: AAK92480.1 .
    AY285780 mRNA. Translation: AAP43112.1 .
    AF536207 mRNA. Translation: AAM97359.1 .
    DQ464183 mRNA. Translation: ABE73157.1 .
    CCDSi CCDS9511.1. [P02462-1 ]
    PIRi S16876. CGHU4B.
    RefSeqi NP_001836.2. NM_001845.4. [P02462-1 ]
    UniGenei Hs.17441.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LI1 X-ray 1.90 A/B/D/E 1441-1669 [» ]
    ProteinModelPortali P02462.
    SMRi P02462. Positions 1442-1669.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107679. 14 interactions.
    IntActi P02462. 24 interactions.
    MINTi MINT-6743187.
    STRINGi 9606.ENSP00000364979.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P02462.

    Polymorphism databases

    DMDMi 125987809.

    Proteomic databases

    MaxQBi P02462.
    PaxDbi P02462.
    PRIDEi P02462.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375820 ; ENSP00000364979 ; ENSG00000187498 . [P02462-1 ]
    GeneIDi 1282.
    KEGGi hsa:1282.
    UCSCi uc001vqw.4. human. [P02462-1 ]

    Organism-specific databases

    CTDi 1282.
    GeneCardsi GC13M110801.
    GeneReviewsi COL4A1.
    HGNCi HGNC:2202. COL4A1.
    HPAi CAB001695.
    HPA054039.
    MIMi 120130. gene.
    175780. phenotype.
    607595. phenotype.
    611773. phenotype.
    neXtProti NX_P02462.
    Orphaneti 73229. Autosomal dominant familial hematuria - retinal arteriolar tortuosity - contractures.
    99810. Familial porencephaly.
    36383. Familial vascular leukoencephalopathy.
    799. Schizencephaly.
    899. Walker-Warburg syndrome.
    PharmGKBi PA26717.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004933.
    KOi K06237.
    OMAi SSMDHGF.
    OrthoDBi EOG7RZ5P3.
    PhylomeDBi P02462.
    TreeFami TF316865.

    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_163699. Scavenging by Class A Receptors.
    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 COL4A1. human.
    EvolutionaryTracei P02462.
    GeneWikii Collagen,_type_IV,_alpha_1.
    GenomeRNAii 1282.
    NextBioi 5181.
    PROi P02462.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02462.
    Bgeei P02462.
    CleanExi HS_COL4A1.
    Genevestigatori P02462.

    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. 21 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. "Structural organization of the gene for the alpha 1 chain of human type IV collagen."
      Soininen R., Huotari M., Ganguly A., Prockop D.J., Tryggvason K.
      J. Biol. Chem. 264:13565-13571(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-555.
    2. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-555 AND HIS-1334.
      Tissue: Brain.
    4. "Completion of the amino acid sequence of the alpha 1 chain of human basement membrane collagen (type IV) reveals 21 non-triplet interruptions located within the collagenous domain."
      Brazel D., Oberbaeumer I., Dieringer H., Babel W., Glanville R.W., Deutzmann R., Kuehn K.
      Eur. J. Biochem. 168:529-536(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-943, VARIANT PRO-555.
      Tissue: Placenta.
    5. "The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter region."
      Soininen R., Huotari M., Hostikka S.L., Prockop D.J., Tryggvason K.
      J. Biol. Chem. 263:17217-17220(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
    6. "Amino acid sequence of the N-terminal aggregation and cross-linking region (7S domain) of the alpha 1 (IV) chain of human basement membrane collagen."
      Glanville R.W., Qian R.Q., Siebold B., Risteli J., Kuehn K.
      Eur. J. Biochem. 152:213-219(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-243.
    7. "Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen."
      Soininen R., Haka-Risku T., Prockop D.J., Tryggvason K.
      FEBS Lett. 225:188-194(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-1257, VARIANT PRO-555.
      Tissue: Placenta.
    8. "Structure of human-basement-membrane (type IV) collagen. Complete amino-acid sequence of a 914-residue-long pepsin fragment from the alpha 1(IV) chain."
      Babel W., Glanville R.W.
      Eur. J. Biochem. 143:545-556(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 534-1447.
    9. "cDNA clones coding for the pro-alpha1(IV) chain of human type IV procollagen reveal an unusual homology of amino acid sequences in two halves of the carboxyl-terminal domain."
      Pihlajaniemi T., Tryggvason K., Myers J.C., Kurkinen M., Lebo R., Cheung M.-C., Prockop D.J., Boyd C.D.
      J. Biol. Chem. 260:7681-7687(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1256-1669.
    10. "Restricted homology between human alpha 1 type IV and other procollagen chains."
      Brinker J.M., Gudas L.J., Loidl H.R., Wang S.-Y., Rosenbloom J., Kefalides N.A., Myers J.C.
      Proc. Natl. Acad. Sci. U.S.A. 82:3649-3653(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1669.
    11. "The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen."
      Siebold B., Deutzmann R., Kuehn K.
      Eur. J. Biochem. 176:617-624(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1441-1669, DISULFIDE BONDS.
      Tissue: Placenta.
    12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION OF ARRESTEN, TISSUE SPECIFICITY.
    13. "Arresten, a collagen-derived inhibitor of angiogenesis."
      Fu J., Bai X., Wang W., Ruan C.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
    14. Peng X., Yin B., Yuan J., Qiang B.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
    15. "Molecular cloning and sequencing of human arresten gene."
      Zheng Q.C., Song Z.F., Zheng Y.W., Li Y.Q., Shu X.
      Zhonghua Shi Yan Wai Ke Za Zhi 19:46-47(2002)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
    16. "Cloning and expression of arresten in Escherichia coli and Pachia pastoris."
      He A.B.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
    17. "Construction of recombinant plasmid and prokaryotic expression in E. coli and biological activity analysis of human placenta arresten gene."
      Zheng J.P., Tang H.Y., Chen X.J., Yu B.F., Xie J., Wu T.C.
      Hepatobiliary Pancreat. Dis. Int. 5:74-79(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION, TISSUE SPECIFICITY.
      Tissue: Placenta.
    18. "Human alpha1 type IV collagen NC1 domain exhibits distinct antiangiogenic activity mediated by alpha1beta1 integrin."
      Sudhakar A., Nyberg P., Keshamouni V.G., Mannam A.P., Li J., Sugimoto H., Cosgrove D., Kalluri R.
      J. Clin. Invest. 115:2801-2810(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RECEPTOR, FUNCTION OF ARRESTEN.
    19. "Characterization of the anti-angiogenic properties of arresten, an alpha1beta1 integrin-dependent collagen-derived tumor suppressor."
      Nyberg P., Xie L., Sugimoto H., Colorado P., Sund M., Holthaus K., Sudhakar A., Salo T., Kalluri R.
      Exp. Cell Res. 314:3292-3305(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RECEPTOR, FUNCTION OF ARRESTEN.
    20. "The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link."
      Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R., Bourenkov G.P., Bartunik H.D., Bode W.
      Proc. Natl. Acad. Sci. U.S.A. 99:6607-6612(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1441-1669, ADDITIONAL INTERCHAIN LINKS.
    21. Cited for: VARIANTS POREN1 SER-749 AND ARG-1236.
    22. "Novel mutations in three families confirm a major role of COL4A1 in hereditary porencephaly."
      Breedveld G., de Coo I.F., Lequin M.H., Arts W.F.M., Heutink P., Gould D.B., John S.W.M., Oostra B., Mancini G.M.S.
      J. Med. Genet. 43:490-495(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS POREN1 ASP-1130 AND ARG-1423.
    23. Cited for: VARIANT BSVDH GLU-562.
    24. Cited for: VARIANT BSVDH ASP-720.
    25. Cited for: VARIANTS HANAC VAL-498; ARG-519 AND GLU-528.
    26. Cited for: INTERCHAIN SULFILIMINE BONDS.
    27. "COL4A1 mutation in a patient with sporadic, recurrent intracerebral hemorrhage."
      Vahedi K., Kubis N., Boukobza M., Arnoult M., Massin P., Tournier-Lasserve E., Bousser M.G.
      Stroke 38:1461-1464(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSVDH ARG-805.
    28. "COL4A1 mutation in two preterm siblings with antenatal onset of parenchymal hemorrhage."
      de Vries L.S., Koopman C., Groenendaal F., Van Schooneveld M., Verheijen F.W., Verbeek E., Witkamp T.D., van der Worp H.B., Mancini G.
      Ann. Neurol. 65:12-18(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT POREN1 ARG-1580.
    29. "Novel COL4A1 mutations associated with HANAC syndrome: a role for the triple helical CB3[IV] domain."
      Plaisier E., Chen Z., Gekeler F., Benhassine S., Dahan K., Marro B., Alamowitch S., Paques M., Ronco P.
      Am. J. Med. Genet. A 152:2550-2555(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HANAC ARG-498; ARG-510 AND LEU-525.
    30. "Ophthalmological features associated with COL4A1 mutations."
      Coupry I., Sibon I., Mortemousque B., Rouanet F., Mine M., Goizet C.
      Arch. Ophthalmol. 128:483-489(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BSVDH ASP-720 AND ARG-755.
    31. "A dominantly inherited mutation in collagen IV A1 (COL4A1) causing childhood onset stroke without porencephaly."
      Shah S., Kumar Y., McLean B., Churchill A., Stoodley N., Rankin J., Rizzu P., van der Knaap M., Jardine P.
      Eur. J. Paediatr. Neurol. 14:182-187(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSVDH ARG-755.
    32. "Sequence variants in COL4A1 and COL4A2 genes in Ecuadorian families with keratoconus."
      Karolak J.A., Kulinska K., Nowak D.M., Pitarque J.A., Molinari A., Rydzanicz M., Bejjani B.A., Gajecka M.
      Mol. Vis. 17:827-843(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LEU-7; PRO-555 AND HIS-1334.

    Entry informationi

    Entry nameiCO4A1_HUMAN
    AccessioniPrimary (citable) accession number: P02462
    Secondary accession number(s): A7E2W4
    , B1AM70, Q1P9S9, Q5VWF6, Q86X41, Q8NF88, Q9NYC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 166 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3