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P53420

- CO4A4_HUMAN

UniProt

P53420 - CO4A4_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP53420.
CleanExiHS_COL4A4.
ExpressionAtlasiP53420. baseline and differential.
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.
GeneTreeiENSGT00770000120455.
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

        10         20         30         40         50
MWSLHIVLMR CSFRLTKSLA TGPWSLILIL FSVQYVYGSG KKYIGPCGGR
60 70 80 90 100
DCSVCHCVPE KGSRGPPGPP GPQGPIGPLG APGPIGLSGE KGMRGDRGPP
110 120 130 140 150
GAAGDKGDKG PTGVPGFPGL DGIPGHPGPP GPRGKPGMSG HNGSRGDPGF
160 170 180 190 200
PGGRGALGPG GPLGHPGEKG EKGNSVFILG AVKGIQGDRG DPGLPGLPGS
210 220 230 240 250
WGAGGPAGPT GYPGEPGLVG PPGQPGRPGL KGNPGVGVKG QMGDPGEVGQ
260 270 280 290 300
QGSPGPTLLV EPPDFCLYKG EKGIKGIPGM VGLPGPPGRK GESGIGAKGE
310 320 330 340 350
KGIPGFPGPR GDPGSYGSPG FPGLKGELGL VGDPGLFGLI GPKGDPGNRG
360 370 380 390 400
HPGPPGVLVT PPLPLKGPPG DPGFPGRYGE TGDVGPPGPP GLLGRPGEAC
410 420 430 440 450
AGMIGPPGPQ GFPGLPGLPG EAGIPGRPDS APGKPGKPGS PGLPGAPGLQ
460 470 480 490 500
GLPGSSVIYC SVGNPGPQGI KGKVGPPGGR GPKGEKGNEG LCACEPGPMG
510 520 530 540 550
PPGPPGLPGR QGSKGDLGLP GWLGTKGDPG PPGAEGPPGL PGKHGASGPP
560 570 580 590 600
GNKGAKGDMV VSRVKGHKGE RGPDGPPGFP GQPGSHGRDG HAGEKGDPGP
610 620 630 640 650
PGDHEDATPG GKGFPGPLGP PGKAGPVGPP GLGFPGPPGE RGHPGVPGHP
660 670 680 690 700
GVRGPDGLKG QKGDTISCNV TYPGRHGPPG FDGPPGPKGF PGPQGAPGLS
710 720 730 740 750
GSDGHKGRPG TPGTAEIPGP PGFRGDMGDP GFGGEKGSSP VGPPGPPGSP
760 770 780 790 800
GVNGQKGIPG DPAFGHLGPP GKRGLSGVPG IKGPRGDPGC PGAEGPAGIP
810 820 830 840 850
GFLGLKGPKG REGHAGFPGV PGPPGHSCER GAPGIPGQPG LPGYPGSPGA
860 870 880 890 900
PGGKGQPGDV GPPGPAGMKG LPGLPGRPGA HGPPGLPGIP GPFGDDGLPG
910 920 930 940 950
PPGPKGPRGL PGFPGFPGER GKPGAEGCPG AKGEPGEKGM SGLPGDRGLR
960 970 980 990 1000
GAKGAIGPPG DEGEMAIISQ KGTPGEPGPP GDDGFPGERG DKGTPGMQGR
1010 1020 1030 1040 1050
RGEPGRYGPP GFHRGEPGEK GQPGPPGPPG PPGSTGLRGF IGFPGLPGDQ
1060 1070 1080 1090 1100
GEPGSPGPPG FSGIDGARGP KGNKGDPASH FGPPGPKGEP GSPGCPGHFG
1110 1120 1130 1140 1150
ASGEQGLPGI QGPRGSPGRP GPPGSSGPPG CPGDHGMPGL RGQPGEMGDP
1160 1170 1180 1190 1200
GPRGLQGDPG IPGPPGIKGP SGSPGLNGLH GLKGQKGTKG ASGLHDVGPP
1210 1220 1230 1240 1250
GPVGIPGLKG ERGDPGSPGI SPPGPRGKKG PPGPPGSSGP PGPAGATGRA
1260 1270 1280 1290 1300
PKDIPDPGPP GDQGPPGPDG PRGAPGPPGL PGSVDLLRGE PGDCGLPGPP
1310 1320 1330 1340 1350
GPPGPPGPPG YKGFPGCDGK DGQKGPVGFP GPQGPHGFPG PPGEKGLPGP
1360 1370 1380 1390 1400
PGRKGPTGLP GPRGEPGPPA DVDDCPRIPG LPGAPGMRGP EGAMGLPGMR
1410 1420 1430 1440 1450
GPSGPGCKGE PGLDGRRGVD GVPGSPGPPG RKGDTGEDGY PGGPGPPGPI
1460 1470 1480 1490 1500
GDPGPKGFGP GYLGGFLLVL HSQTDQEPTC PLGMPRLWTG YSLLYLEGQE
1510 1520 1530 1540 1550
KAHNQDLGLA GSCLPVFSTL PFAYCNIHQV CHYAQRNDRS YWLASAAPLP
1560 1570 1580 1590 1600
MMPLSEEAIR PYVSRCAVCE APAQAVAVHS QDQSIPPCPQ TWRSLWIGYS
1610 1620 1630 1640 1650
FLMHTGAGDQ GGGQALMSPG SCLEDFRAAP FLECQGRQGT CHFFANKYSF
1660 1670 1680 1690
WLTTVKADLQ FSSAPAPDTL KESQAQRQKI SRCQVCVKYS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00770000120455.
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

Bgeei P53420.
CleanExi HS_COL4A4.
ExpressionAtlasi P53420. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 156 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