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Protein

Collagen alpha-5(IV) chain

Gene

COL4A5

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-5(IV) chain
Gene namesi
Name:COL4A5
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

A defect in COL4A5 has been found to be the cause of canine X-linked hereditary nephritis (HN), a disease similar to that in humans (also referred to as Alport syndrome) characterized by progressive renal failure and neurosensory deafness.

Keywords - Diseasei

Alport syndrome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 16911665Collagen alpha-5(IV) chainPRO_0000005851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi451 – 451InterchainPROSITE-ProRule annotation
Disulfide bondi481 – 481InterchainPROSITE-ProRule annotation
Disulfide bondi484 – 484InterchainPROSITE-ProRule annotation
Disulfide bondi1482 ↔ 1573Or C-1482 with C-1570PROSITE-ProRule annotation
Disulfide bondi1515 ↔ 1570Or C-1515 with C-1573PROSITE-ProRule annotation
Disulfide bondi1527 ↔ 1533PROSITE-ProRule annotation
Cross-linki1555 – 1555S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1673)By similarity
Disulfide bondi1592 ↔ 1687Or C-1592 with C-1684PROSITE-ProRule annotation
Disulfide bondi1626 ↔ 1684Or C-1626 with C-1687PROSITE-ProRule annotation
Disulfide bondi1638 ↔ 1644PROSITE-ProRule annotation
Cross-linki1673 – 1673S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1555)By similarity

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

PaxDbiQ28247.

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

STRINGi9615.ENSCAFP00000026629.

Structurei

3D structure databases

ProteinModelPortaliQ28247.
SMRiQ28247. Positions 1464-1691.
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
Regioni27 – 4115Nonhelical region (NC2)Add
BLAST
Regioni42 – 14621421Triple-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

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiQ28247.
KOiK06237.

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.

Q28247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLRGVSLAA GWFLLALSLW GQPAEAAACY GCSPGSKCDC SGVKGEKGER
60 70 80 90 100
GFPGLEGHPG LPGFPGPEGP PGPRGQKGDD GIRGPPGPKG IRGPPGLPGF
110 120 130 140 150
PGTPGLPGMP GHDGAPGPQG IPGCNGTKGE RGFPGSPGFP GLEGPPGPPG
160 170 180 190 200
IPGMKGEPGS IIMSSLPGPK GNPGYPGPPG IQGPAGPTGL PGPIGPPGPP
210 220 230 240 250
GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP PGQISEQKRP
260 270 280 290 300
IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGMKGEKGE QGEPGKRGKP
310 320 330 340 350
GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDIGSTG PPGLVIPRPG
360 370 380 390 400
TGVTVGEKGN MGLPGLPGEK GERGFPGIQG PPGLPGPPGT AVMGPPGPPG
410 420 430 440 450
FPGERGQKGD EGPPGISIPG FPGLDGQPGA PGLRGPPGPP GPHISPSDEI
460 470 480 490 500
CETGPPGPPG SPGDRGLQGE QGVKGDKGDT CFNCIGTGVS GPRGQPGLPG
510 520 530 540 550
LPGPPGSLGF PGQKGEKGHA GLTGPKGLTG IPGAPGPPGF PGSKGEPGDV
560 570 580 590 600
LTFPGMKGDK GELGYPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGIAFKG
610 620 630 640 650
ERGPPGNPGL PGLPGNRGPM GPVGFGPPGP VGEKGIQGVA GNPGQPGIPG
660 670 680 690 700
PKGDPGQTIT QPGKPGLPGN PGRHGEVGLP GDPGLPGPPG LPGIPGNKGE
710 720 730 740 750
PGIPGIGLPG PPGPKGFPGI QGPPGAPGTP GRIGLEGPSG PPGFPGPKGE
760 770 780 790 800
PGLGLPGPPG PPGLPGFKGT LGPKGDRGFP GPPGLPGRTG LDGLPGPKGD
810 820 830 840 850
VGPKGQPGPM GPPGLPGIGV QGPPGPPGIP GPVGEPGLHG IPGEKGDPGP
860 870 880 890 900
PGFDVLGPPG ERGSPGIPGA PGPMGPPGTP GLPGKAGASG FPGAKGEMGM
910 920 930 940 950
MGPPGPPGPL GIPGRSGVPG LKGDNGLQGQ PGPPGPEGEK GGKGEPGLPG
960 970 980 990 1000
PPGPVDPDLL GSKGEKGDPG LPGIPGVSGP KGYQGLPGDP GQPGLSGQPG
1010 1020 1030 1040 1050
LPGPSGPKGN PGLPGKPGLT GPPGLKGSIG DMGFPGPQGV KGSPGPPGVP
1060 1070 1080 1090 1100
GQPGSPGLPG QKGEKGDPGV SGIGLPGLPG PKGEAGLPGY PGNPGIKGSM
1110 1120 1130 1140 1150
GDTGLPGLPG TPGAKGQPGL PGFPGTPGLP GPKGINGPPG NPGLPGEPGP
1160 1170 1180 1190 1200
VGGGGRPGPP GPPGEKGNPG QDGIPGPAGQ KGEPGQPGFG IPGPPGLPGL
1210 1220 1230 1240 1250
SGQKGDGGLP GIPGNPGLPG PKGEPGFQGF PGVQGPPGPP GSPGPALEGP
1260 1270 1280 1290 1300
KGNPGPQGPP GRPGPTGFQG LPGPEGPRGL PGNGGIKGER GNPGQPGQPG
1310 1320 1330 1340 1350
LPGLKGDQGP PGIQGNPGRP GLNGMKGDPG LPGVPGFPGM KGPSGVPGSA
1360 1370 1380 1390 1400
GPEGDPGLVG PPGPPGLPGP SGQSIIIKGD VGPPGIPGQP GLKGLPGLPG
1410 1420 1430 1440 1450
PQGLPGPIGP PGDPGRNGLP GFDGAGGRKG DPGLPGQPGT RGLDGPPGPD
1460 1470 1480 1490 1500
GMQGPPGPPG TSSIAHGFLI TRHSQTTDAP QCPHGTVQIY EGFSLLYVQG
1510 1520 1530 1540 1550
NKRAHGQDLG TAGSCLRRFS TMPFMFCNIN NVCNFASRND YSYWLSTPEP
1560 1570 1580 1590 1600
MPMSMEPLKG QSIQPFISRC AVCEAPAVVI AVHSQTIQIP HCPHGWDSLW
1610 1620 1630 1640 1650
IGYSFMMHTS AGAEGSGQAL ASPGSCLEEF RSAPFIECHG RGTCNYYANS
1660 1670 1680 1690
YSFWLATVDV SDMFSKPQSE TLKAGDLRTR ISRCQVCMKR T
Length:1,691
Mass (Da):162,237
Last modified:April 12, 2005 - v2
Checksum:i513DB6DAB4C3C68D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti925 – 9251N → D in AAB60258 (PubMed:8171024).Curated
Sequence conflicti1158 – 11581G → W in AAB60258 (PubMed:8171024).Curated
Sequence conflicti1265 – 12706Missing in AAB60258 (PubMed:8171024).Curated
Sequence conflicti1575 – 15751A → R in AAB60258 (PubMed:8171024).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF470624 mRNA. Translation: AAO33458.2.
U07888 mRNA. Translation: AAB60258.1.
PIRiA55267.
RefSeqiNP_001002979.1. NM_001002979.1.
UniGeneiCfa.177.

Genome annotation databases

GeneIDi403466.
KEGGicfa:403466.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF470624 mRNA. Translation: AAO33458.2.
U07888 mRNA. Translation: AAB60258.1.
PIRiA55267.
RefSeqiNP_001002979.1. NM_001002979.1.
UniGeneiCfa.177.

3D structure databases

ProteinModelPortaliQ28247.
SMRiQ28247. Positions 1464-1691.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000026629.

Proteomic databases

PaxDbiQ28247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403466.
KEGGicfa:403466.

Organism-specific databases

CTDi1287.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiQ28247.
KOiK06237.

Miscellaneous databases

NextBioi20816982.

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]
ProtoNetiSearch...

Publicationsi

  1. "Genetic cause of X-linked Alport syndrome in a family of domestic dogs."
    Cox M.L., Lees G.E., Kashtan C.E., Murphy K.E.
    Mamm. Genome 14:396-403(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISEASE.
  2. "Canine X chromosome-linked hereditary nephritis: a genetic model for human X-linked hereditary nephritis resulting from a single base mutation in the gene encoding the alpha 5 chain of collagen type IV."
    Zheng K., Thorner P.S., Marrano P., Baumal R., McInnes R.R.
    Proc. Natl. Acad. Sci. U.S.A. 91:3989-3993(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 925-1684, DISEASE.
    Strain: Samoyed.
    Tissue: Kidney.

Entry informationi

Entry nameiCO4A5_CANLF
AccessioniPrimary (citable) accession number: Q28247
Secondary accession number(s): Q866Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 12, 2005
Last modified: December 9, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.