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Protein

Collagen alpha-1(IV) chain

Gene

COL4A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.By similarity
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.By similarity

GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-BTA-1442490 Collagen degradation
R-BTA-1474244 Extracellular matrix organization
R-BTA-1650814 Collagen biosynthesis and modifying enzymes
R-BTA-186797 Signaling by PDGF
R-BTA-2022090 Assembly of collagen fibrils and other multimeric structures
R-BTA-216083 Integrin cell surface interactions
R-BTA-2214320 Anchoring fibril formation
R-BTA-3000157 Laminin interactions
R-BTA-3000171 Non-integrin membrane-ECM interactions
R-BTA-419037 NCAM1 interactions
R-BTA-8948216 Collagen chain trimerization

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(IV) chain
Cleaved into the following chain:
Gene namesi
Name:COL4A1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 12

Organism-specific databases

VGNCiVGNC:50081 COL4A1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
ChainiPRO_000005939928 – 1669Collagen alpha-1(IV) chainAdd BLAST1642
PropeptideiPRO_000044182428 – 172N-terminal propeptide (7S domain)By similarityAdd BLAST145
ChainiPRO_00004418251445 – 1669ArrestenAdd BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2043-hydroxyproline1 Publication1
Modified residuei2073-hydroxyproline1 Publication1
Modified residuei2103-hydroxyproline1 Publication1
Modified residuei5873-hydroxyproline1 Publication1
Modified residuei6023-hydroxyproline1 Publication1
Modified residuei6034-hydroxyprolineBy similarity1
Modified residuei6053-hydroxyproline1 Publication1
Modified residuei6064-hydroxyprolineBy similarity1
Modified residuei6234-hydroxyprolineBy similarity1
Modified residuei6264-hydroxyprolineBy similarity1
Modified residuei6294-hydroxyprolineBy similarity1
Modified residuei6324-hydroxyprolineBy similarity1
Modified residuei6473-hydroxyproline1 Publication1
Modified residuei12143-hydroxyproline1 Publication1
Modified residuei14243-hydroxyproline1 Publication1
Disulfide bondi1460 ↔ 1551PROSITE-ProRule annotation1 Publication
Disulfide bondi1493 ↔ 1548PROSITE-ProRule annotation1 Publication
Disulfide bondi1505 ↔ 1511PROSITE-ProRule annotation1 Publication
Cross-linki1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)1 Publication
Disulfide bondi1570 ↔ 1665PROSITE-ProRule annotation1 Publication
Disulfide bondi1604 ↔ 1662PROSITE-ProRule annotation1 Publication
Disulfide bondi1616 ↔ 1622PROSITE-ProRule annotation1 Publication
Cross-linki1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)1 Publication

Post-translational modificationi

Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases. The modified lysines can be O-glycosylated.By similarity
Contains 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.By similarity
Contains 3-hydroxyproline (PubMed:24368846). This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline (By similarity).By similarity1 Publication
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.By similarity
The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues (PubMed:19729652). These cross-links are important for the mechanical stability of the basement membrane (By similarity).By similarity1 Publication
Proteolytic processing produces the C-terminal NC1 peptide, arresten.By similarity

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiQ7SIB2

PTM databases

GlyConnecti108

Expressioni

Gene expression databases

BgeeiENSBTAG00000012849

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.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000035211

Structurei

Secondary structure

11669
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1446 – 1451Combined sources6
Beta strandi1453 – 1456Combined sources4
Beta strandi1465 – 1478Combined sources14
Beta strandi1481 – 1484Combined sources4
Helixi1490 – 1492Combined sources3
Beta strandi1493 – 1496Combined sources4
Beta strandi1502 – 1505Combined sources4
Beta strandi1511 – 1514Combined sources4
Beta strandi1519 – 1524Combined sources6
Helixi1538 – 1544Combined sources7
Beta strandi1547 – 1555Combined sources9
Beta strandi1557 – 1561Combined sources5
Beta strandi1563 – 1566Combined sources4
Beta strandi1575 – 1587Combined sources13
Helixi1589 – 1591Combined sources3
Beta strandi1593 – 1595Combined sources3
Helixi1601 – 1603Combined sources3
Beta strandi1604 – 1607Combined sources4
Beta strandi1613 – 1617Combined sources5
Beta strandi1620 – 1623Combined sources4
Beta strandi1629 – 1634Combined sources6
Helixi1638 – 1640Combined sources3
Beta strandi1648 – 1650Combined sources3
Helixi1656 – 1658Combined sources3
Beta strandi1661 – 1666Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M3DX-ray2.00A/B/D/E/G/H/J/K1441-1669[»]
1T60X-ray1.50A/B/D/E/G/H/J/K/M/N/P/Q/S/T/V/W1441-1669[»]
1T61X-ray1.50A/B/D/E1441-1669[»]
ProteinModelPortaliQ7SIB2
SMRiQ7SIB2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIB2

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1445 – 1669Collagen IV NC1PROSITE-ProRule annotationAdd BLAST225

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 1440Triple-helical regionCuratedAdd BLAST1268

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.Curated

Sequence similaritiesi

Belongs to the type IV collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00900000140804
HOGENOMiHOG000085652
HOVERGENiHBG004933
InParanoidiQ7SIB2
OMAiVIGFPGM
OrthoDBiEOG091G0613
TreeFamiTF316865

Family and domain databases

Gene3Di2.170.240.10, 1 hit
InterProiView protein in InterPro
IPR008160 Collagen
IPR001442 Collagen_IV_NC
IPR036954 Collagen_IV_NC_sf
IPR016187 CTDL_fold
PfamiView protein in Pfam
PF01413 C4, 2 hits
PF01391 Collagen, 17 hits
SMARTiView protein in SMART
SM00111 C4, 2 hits
SUPFAMiSSF56436 SSF56436, 2 hits
PROSITEiView protein in PROSITE
PS51403 NC1_IV, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q7SIB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPRLGVWLL LLLAALLLHE ESSRAAAKGG CAGSGCGKCD CHGVKGQKGE
60 70 80 90 100
RGLPGLQGVI GFPGMQGPEG PQGPPGQKGD TGEPGLPGTK GTRGPSGVPG
110 120 130 140 150
YPGNPGLPGI PGQDGPPGPP GIPGCNGTKG ERGPVGPPGL PGFAGNPGPP
160 170 180 190 200
GLPGMKGDPG EILGHIPGTL LKGERGYPGQ PGAPGSPGLP GLQGPVGPPG
210 220 230 240 250
FTGPPGPPGP PGPPGEKGQM GLSFQGPKGE KGDQGVSGPP GLPGQAQVIT
260 270 280 290 300
KGDTAMRGEK GQKGEPGFPG LPGFGEKGEP GKPGPRGKPG KDGEKGEKGS
310 320 330 340 350
PGFPGDSGYP GQPGQDGLKG EKGEAGPPGL PGTVIGTGPL GEKGEPGYPG
360 370 380 390 400
GPGAKGETGP KGFPGIPGQP GPPGFPTPGL IGAPGFPGDR GEKGEPGLPG
410 420 430 440 450
VSLPGPSGRD GLPGPPGPPG PPGQPGHTNG IVECQPGPPG DQGPPGIPGQ
460 470 480 490 500
PGLTGEVGEK GQKGDSCLVC DTAELRGPPG PQGPPGEIGF PGQPGAKGDR
510 520 530 540 550
GLPGRDGLEG LPGPQGAPGL MGQPGAKGEP GEIYFDIRLK GDKGDPGFPG
560 570 580 590 600
QPGMPGRAGS PGRDGQPGLP GPRGSPGSVG LKGERGPPGG VGFPGSRGDI
610 620 630 640 650
GPPGPPGFGP IGPIGDKGQI GFPGTPGAPG QPGPKGEAGK VVPLPGPPGA
660 670 680 690 700
EGLPGSPGFQ GPQGDRGFPG SPGRPGLPGE KGAIGQPGIG FPGPPGPKGV
710 720 730 740 750
DGLPGDAGPP GNPGRQGFNG LPGNPGPPGQ KGEPGVGLPG LKGLPGIPGI
760 770 780 790 800
PGTPGEKGNV GGPGIPGEHG AIGPPGLQGL RGDPGPPGFQ GPKGAPGVPG
810 820 830 840 850
IGPPGAMGPP GGQGPPGSSG PPGVKGEKGF PGFPGLDMPG PKGDKGSQGL
860 870 880 890 900
PGLTGQSGLP GLPGQQGTPG QPGIPGPKGE MGVMGTPGQP GSPGPAGVPG
910 920 930 940 950
LPGAKGDHGF PGSSGPRGDP GFKGDKGDVG LPGKPGSMDK VDMGSMKGEK
960 970 980 990 1000
GDQGEKGQTG PTGDKGSRGD PGTPGVPGKD GQAGHPGQPG PKGDPGVSGI
1010 1020 1030 1040 1050
PGAPGLPGPK GSAGGMGLPG MPGPKGVAGI PGPQGIPGLP GDKGAKGEKG
1060 1070 1080 1090 1100
QAGLPGIGIP GRPGDKGDQG LAGFPGSPGE KGEKGSTGIP GMPGSPGPKG
1110 1120 1130 1140 1150
SPGSVGYPGS PGLPGEKGDK GLPGLDGIPG IKGEAGLPGK PGPTGPAGQK
1160 1170 1180 1190 1200
GEPGSDGIPG SVGEKGESGL PGRGFPGFPG SKGDKGSKGD VGFPGLSGSP
1210 1220 1230 1240 1250
GIPGSKGEQG FMGPPGPQGQ PGLPGTPGHA VEGPKGDRGP QGQPGLPGRP
1260 1270 1280 1290 1300
GPMGPPGLPG LEGLKGERGN PGWPGTPGAP GPKGDPGFQG MPGIGGSPGI
1310 1320 1330 1340 1350
TGAKGDVGPP GVPGFHGQKG APGLQGVKGD QGDQGFPGTK GLPGPPGPPG
1360 1370 1380 1390 1400
PFSIIKGEPG LPGPEGPAGL KGLQGPPGPK GQQGVTGSVG LPGPPGEPGF
1410 1420 1430 1440 1450
DGAPGQKGET GPFGPPGPRG FPGPPGPDGL PGSMGPPGTP SVDHGFLVTR
1460 1470 1480 1490 1500
HSQTTDDPQC PPGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM
1510 1520 1530 1540 1550
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPITGEN IRPFISRCAV
1560 1570 1580 1590 1600
CEAPAMVMAV HSQTIQIPQC PTGWSSLWIG YSFVMHTSAG AEGSGQALAS
1610 1620 1630 1640 1650
PGSCLEEFRS APFIECHGRG TCNYYANAYS FWLATIERSE MFKKPTPSTL
1660
KAGELRTHVS RCQVCMRRT
Length:1,669
Mass (Da):160,412
Last modified:October 25, 2017 - v2
Checksum:iAFC2A53A7BE484B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02034907 Genomic DNA No translation available.
DAAA02034908 Genomic DNA No translation available.
DAAA02034909 Genomic DNA No translation available.
UniGeneiBt.32410

Genome annotation databases

EnsembliENSBTAT00000035335; ENSBTAP00000035211; ENSBTAG00000012849

Similar proteinsi

Entry informationi

Entry nameiCO4A1_BOVIN
AccessioniPrimary (citable) accession number: Q7SIB2
Secondary accession number(s): G1K238
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 25, 2017
Last modified: April 25, 2018
This is version 93 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health