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Q01955

- CO4A3_HUMAN

UniProt

Q01955 - CO4A3_HUMAN

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Protein

Collagen alpha-3(IV) chain

Gene

COL4A3

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.
Tumstatin, a cleavage fragment corresponding to the collagen alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity; these two anti-tumor properties may be regulated via RGD-independent ITGB3-mediated mechanisms.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1426 – 14272Cleavage; by collagenaseBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. integrin binding Source: UniProtKB
  3. metalloendopeptidase inhibitor activity Source: UniProtKB
  4. structural molecule activity Source: ProtInc

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. axon guidance Source: Reactome
  3. blood circulation Source: ProtInc
  4. cell adhesion Source: UniProtKB-KW
  5. cell proliferation Source: UniProtKB
  6. cell surface receptor signaling pathway Source: UniProtKB
  7. collagen catabolic process Source: Reactome
  8. endothelial cell apoptotic process Source: UniProtKB
  9. extracellular matrix disassembly Source: Reactome
  10. extracellular matrix organization Source: Reactome
  11. glomerular basement membrane development Source: UniProtKB
  12. negative regulation of angiogenesis Source: UniProtKB
  13. negative regulation of cell proliferation Source: ProtInc
  14. negative regulation of endopeptidase activity Source: GOC
  15. sensory perception of sound Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

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-3(IV) chain
Alternative name(s):
Goodpasture antigen
Cleaved into the following chain:
Gene namesi
Name:COL4A3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2204. COL4A3.

Subcellular locationi

Secretedextracellular spaceextracellular matrixbasement membrane
Note: Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).By similarity

GO - Cellular componenti

  1. basement membrane 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

Autoantibodies against the NC1 domain of alpha 3(IV) are found in Goodpasture syndrome, an autoimmune disease of lung and kidney.
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 varianti297 – 2971G → E in APSAR. 1 Publication
VAR_011204
Natural varianti407 – 4071G → R in APSAR. 1 Publication
VAR_011206
Natural varianti532 – 5321G → D in APSAR. 1 Publication
VAR_030945
Natural varianti640 – 6401G → R in APSAR. 1 Publication
VAR_011210
Natural varianti739 – 7391G → R in APSAR. 1 Publication
VAR_030946
Natural varianti853 – 8531G → R in APSAR. 1 Publication
VAR_030947
Natural varianti1207 – 12071G → E in APSAR; in isolated microhematuria at heterozygosity. 1 Publication
VAR_011212
Natural varianti1215 – 12151R → Q in APSAR; unknown pathological significance. 1 Publication
VAR_011213
Natural varianti1216 – 12161G → R in APSAR. 1 Publication
VAR_030950
Natural varianti1277 – 12771G → S in APSAR. 1 Publication
Corresponds to variant rs190598500 [ dbSNP | Ensembl ].
VAR_011215
Natural varianti1330 – 13301I → T in APSAR; unknown pathological significance. 1 Publication
VAR_011216
Natural varianti1334 – 13341G → E in APSAR. 1 Publication
VAR_011217
Natural varianti1347 – 13471D → E in APSAR; unknown pathological significance. 1 Publication
Corresponds to variant rs73996414 [ dbSNP | Ensembl ].
VAR_011218
Natural varianti1661 – 16611R → C in APSAR. 1 Publication
VAR_011219
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti985 – 9851G → V in BFH. 1 Publication
VAR_030948
Natural varianti1015 – 10151G → E in BFH. 1 Publication
VAR_030949
Alport syndrome, autosomal dominant (APSAD) [MIM:104200]: 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 varianti1167 – 11671G → R in APSAD; in isolated microhematuria at heterozygosity. 1 Publication
VAR_011211

Keywords - Diseasei

Alport syndrome, Deafness, Disease mutation

Organism-specific databases

MIMi104200. phenotype.
141200. phenotype.
203780. phenotype.
Orphaneti88918. Autosomal dominant Alport syndrome.
88919. Autosomal recessive Alport syndrome.
97562. Benign familial hematuria.
PharmGKBiPA26719.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 16701642Collagen alpha-3(IV) chainPRO_0000005844Add
BLAST
Chaini1426 – 1670245TumstatinPRO_0000279684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
Cross-linki1414 – 1414Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Disulfide bondi1460 ↔ 1551Or C-1460 with C-1548PROSITE-ProRule annotation
Disulfide bondi1493 ↔ 1548Or C-1493 with C-1551PROSITE-ProRule annotation
Disulfide bondi1505 ↔ 1511PROSITE-ProRule annotation
Cross-linki1533 – 1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)By similarity
Disulfide bondi1570 ↔ 1665Or C-1570 with C-1662PROSITE-ProRule annotation
Disulfide bondi1604 ↔ 1662Or C-1604 with C-1665PROSITE-ProRule annotation
Disulfide bondi1616 ↔ 1622PROSITE-ProRule annotation
Cross-linki1651 – 1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)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.
Isoform 2 contains an additional N-linked glycosylation site.
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
Phosphorylated by the Goodpasture antigen-binding protein/COL4A3BP.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ01955.
PaxDbiQ01955.
PRIDEiQ01955.

PTM databases

PhosphoSiteiQ01955.

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. According to PubMed:8083201, alpha 3 type IV collagen is not detected in heart, brain, placenta, liver, pancreas, extrasynaptic muscle fibers, endoneurial and perineurial nerves, fetal brain, fetal heart and fetal liver. According to PubMed:7523402, alpha 3 type IV collagen is strongly expressed in pancreas, neuroretina and calvaria and not expressed in adrenal, ileum and skin. Isoform 1 and isoform 3 are strongly expressed in kidney, lung, suprarenal capsule, muscle and spleen, in each of these tissues isoform 1 is more abundant than isoform 3. Isoform 1 and isoform 3 are expressed at low levels in artery, fat, pericardium and peripherical nerve, but not in placenta, mesangium, skin, pleura and cultured umbilical endothelial cells.3 Publications

Gene expression databases

BgeeiQ01955.
CleanExiHS_COL4A3.
ExpressionAtlasiQ01955. baseline and differential.
GenevestigatoriQ01955.

Organism-specific databases

HPAiHPA042064.

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 promoter, respectively. Interacts with COL4A3BP AND ITGB3. Associates with LAMB2 at the neuromuscular junction and in GBM (By similarity).By similarity

Protein-protein interaction databases

BioGridi107682. 3 interactions.
IntActiQ01955. 1 interaction.
STRINGi9606.ENSP00000379823.

Structurei

3D structure databases

ProteinModelPortaliQ01955.
SMRiQ01955. Positions 1445-1668.
ModBaseiSearch...
MobiDBiSearch...

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
Regioni29 – 42147S domainAdd
BLAST
Regioni43 – 14381396Triple-helical regionAdd
BLAST
Regioni1427 – 144418Epitope recognized by Goodpasture antibodiesAdd
BLAST
Regioni1479 – 155779Required for the anti-angiogenic activity of tumstatinAdd
BLAST
Regioni1610 – 162819Required for the anti-tumor cell activity of tumstatinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi791 – 7933Cell attachment siteSequence Analysis
Motifi996 – 9983Cell attachment siteSequence Analysis
Motifi1154 – 11563Cell attachment siteSequence Analysis
Motifi1306 – 13083Cell attachment siteSequence Analysis
Motifi1345 – 13473Cell attachment siteSequence Analysis
Motifi1432 – 14343Cell 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.
HOVERGENiHBG004933.
InParanoidiQ01955.
KOiK06237.
OMAiSPGCPGK.
OrthoDBiEOG7RZ5P3.
PhylomeDBiQ01955.
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. 22 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: The majority of isoforms differ in the C-terminal part of the NC1 domain.

Isoform 1 (identifier: Q01955-1) [UniParc]FASTAAdd to Basket

Also known as: GP

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

        10         20         30         40         50
MSARTAPRPQ VLLLPLLLVL LAAAPAASKG CVCKDKGQCF CDGAKGEKGE
60 70 80 90 100
KGFPGPPGSP GQKGFTGPEG LPGPQGPKGF PGLPGLTGSK GVRGISGLPG
110 120 130 140 150
FSGSPGLPGT PGNTGPYGLV GVPGCSGSKG EQGFPGLPGT LGYPGIPGAA
160 170 180 190 200
GLKGQKGAPA KEEDIELDAK GDPGLPGAPG PQGLPGPPGF PGPVGPPGPP
210 220 230 240 250
GFFGFPGAMG PRGPKGHMGE RVIGHKGERG VKGLTGPPGP PGTVIVTLTG
260 270 280 290 300
PDNRTDLKGE KGDKGAMGEP GPPGPSGLPG ESYGSEKGAP GDPGLQGKPG
310 320 330 340 350
KDGVPGFPGS EGVKGNRGFP GLMGEDGIKG QKGDIGPPGF RGPTEYYDTY
360 370 380 390 400
QEKGDEGTPG PPGPRGARGP QGPSGPPGVP GSPGSSRPGL RGAPGWPGLK
410 420 430 440 450
GSKGERGRPG KDAMGTPGSP GCAGSPGLPG SPGPPGPPGD IVFRKGPPGD
460 470 480 490 500
HGLPGYLGSP GIPGVDGPKG EPGLLCTQCP YIPGPPGLPG LPGLHGVKGI
510 520 530 540 550
PGRQGAAGLK GSPGSPGNTG LPGFPGFPGA QGDPGLKGEK GETLQPEGQV
560 570 580 590 600
GVPGDPGLRG QPGRKGLDGI PGTPGVKGLP GPKGELALSG EKGDQGPPGD
610 620 630 640 650
PGSPGSPGPA GPAGPPGYGP QGEPGLQGTQ GVPGAPGPPG EAGPRGELSV
660 670 680 690 700
STPVPGPPGP PGPPGHPGPQ GPPGIPGSLG KCGDPGLPGP DGEPGIPGIG
710 720 730 740 750
FPGPPGPKGD QGFPGTKGSL GCPGKMGEPG LPGKPGLPGA KGEPAVAMPG
760 770 780 790 800
GPGTPGFPGE RGNSGEHGEI GLPGLPGLPG TPGNEGLDGP RGDPGQPGPP
810 820 830 840 850
GEQGPPGRCI EGPRGAQGLP GLNGLKGQQG RRGKTGPKGD PGIPGLDRSG
860 870 880 890 900
FPGETGSPGI PGHQGEMGPL GQRGYPGNPG ILGPPGEDGV IGMMGFPGAI
910 920 930 940 950
GPPGPPGNPG TPGQRGSPGI PGVKGQRGTP GAKGEQGDKG NPGPSEISHV
960 970 980 990 1000
IGDKGEPGLK GFAGNPGEKG NRGVPGMPGL KGLKGLPGPA GPPGPRGDLG
1010 1020 1030 1040 1050
STGNPGEPGL RGIPGSMGNM GMPGSKGKRG TLGFPGRAGR PGLPGIHGLQ
1060 1070 1080 1090 1100
GDKGEPGYSE GTRPGPPGPT GDPGLPGDMG KKGEMGQPGP PGHLGPAGPE
1110 1120 1130 1140 1150
GAPGSPGSPG LPGKPGPHGD LGFKGIKGLL GPPGIRGPPG LPGFPGSPGP
1160 1170 1180 1190 1200
MGIRGDQGRD GIPGPAGEKG ETGLLRAPPG PRGNPGAQGA KGDRGAPGFP
1210 1220 1230 1240 1250
GLPGRKGAMG DAGPRGPTGI EGFPGPPGLP GAIIPGQTGN RGPPGSRGSP
1260 1270 1280 1290 1300
GAPGPPGPPG SHVIGIKGDK GSMGHPGPKG PPGTAGDMGP PGRLGAPGTP
1310 1320 1330 1340 1350
GLPGPRGDPG FQGFPGVKGE KGNPGFLGSI GPPGPIGPKG PPGVRGDPGT
1360 1370 1380 1390 1400
LKIISLPGSP GPPGTPGEPG MQGEPGPPGP PGNLGPCGPR GKPGKDGKPG
1410 1420 1430 1440 1450
TPGPAGEKGN KGSKGEPGPA GSDGLPGLKG KRGDSGSPAT WTTRGFVFTR
1460 1470 1480 1490 1500
HSQTTAIPSC PEGTVPLYSG FSFLFVQGNQ RAHGQDLGTL GSCLQRFTTM
1510 1520 1530 1540 1550
PFLFCNVNDV CNFASRNDYS YWLSTPALMP MNMAPITGRA LEPYISRCTV
1560 1570 1580 1590 1600
CEGPAIAIAV HSQTTDIPPC PHGWISLWKG FSFIMFTSAG SEGTGQALAS
1610 1620 1630 1640 1650
PGSCLEEFRA SPFLECHGRG TCNYYSNSYS FWLASLNPER MFRKPIPSTV
1660 1670
KAGELEKIIS RCQVCMKKRH
Length:1,670
Mass (Da):161,813
Last modified:March 6, 2007 - v3
Checksum:iAA65D50903D82B99
GO
Isoform 2 (identifier: Q01955-2) [UniParc]FASTAAdd to Basket

Also known as: V, GP-V

The sequence of this isoform differs from the canonical sequence as follows:
     1586-1670: FTSAGSEGTG...RCQVCMKKRH → KAYSINCESW...NKVMTEHAVI

Show »
Length:1,637
Mass (Da):158,336
Checksum:i92396B115CEA21DF
GO
Isoform 3 (identifier: Q01955-3) [UniParc]FASTAAdd to Basket

Also known as: L5, GP-III, GP-III/V

The sequence of this isoform differs from the canonical sequence as follows:
     1488-1670: GTLGSCLQRF...RCQVCMKKRH → DALFVKVLRSP

Show »
Length:1,498
Mass (Da):142,741
Checksum:i74CF6C2B17B98686
GO
Isoform 4 (identifier: Q01955-4) [UniParc]FASTAAdd to Basket

Also known as: GP-III/IV/V

The sequence of this isoform differs from the canonical sequence as follows:
     1488-1670: GTLGSCLQRF...RCQVCMKKRH → ESLFHQL

Show »
Length:1,494
Mass (Da):142,369
Checksum:iC24C75A6029B73C8
GO
Isoform 5 (identifier: Q01955-5) [UniParc]FASTAAdd to Basket

Also known as: GP-II/III/IV/V

The sequence of this isoform differs from the canonical sequence as follows:
     1418-1424: GPAGSDG → ESLFHQL
     1425-1670: Missing.

Show »
Length:1,424
Mass (Da):135,079
Checksum:i80BA77353C7013C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti911 – 9111T → R in CAC36101. (PubMed:11134255)Curated
Sequence conflicti1539 – 15391R → I in AAA18942. (PubMed:8294492)Curated
Sequence conflicti1594 – 15941T → A in AAB19637. (PubMed:1882840)Curated
Sequence conflicti1663 – 16642QV → HL in AAA52044. 1 PublicationCurated
Isoform 2 (identifier: Q01955-2)
Sequence conflicti1539 – 15391R → I in AAA18942. (PubMed:8294492)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431G → R.1 Publication
Corresponds to variant rs13424243 [ dbSNP | Ensembl ].
VAR_011202
Natural varianti141 – 1411L → P.2 Publications
Corresponds to variant rs10178458 [ dbSNP | Ensembl ].
VAR_030944
Natural varianti162 – 1621E → G.1 Publication
Corresponds to variant rs6436669 [ dbSNP | Ensembl ].
VAR_011203
Natural varianti297 – 2971G → E in APSAR. 1 Publication
VAR_011204
Natural varianti326 – 3261D → Y.1 Publication
Corresponds to variant rs55703767 [ dbSNP | Ensembl ].
VAR_011205
Natural varianti407 – 4071G → R in APSAR. 1 Publication
VAR_011206
Natural varianti408 – 4081R → H.1 Publication
Corresponds to variant rs34505188 [ dbSNP | Ensembl ].
VAR_011207
Natural varianti451 – 4511H → R.1 Publication
Corresponds to variant rs11677877 [ dbSNP | Ensembl ].
VAR_011208
Natural varianti532 – 5321G → D in APSAR. 1 Publication
VAR_030945
Natural varianti574 – 5741P → L.1 Publication
Corresponds to variant rs28381984 [ dbSNP | Ensembl ].
VAR_011209
Natural varianti640 – 6401G → R in APSAR. 1 Publication
VAR_011210
Natural varianti739 – 7391G → R in APSAR. 1 Publication
VAR_030946
Natural varianti834 – 8341K → R.
Corresponds to variant rs56226424 [ dbSNP | Ensembl ].
VAR_061118
Natural varianti853 – 8531G → R in APSAR. 1 Publication
VAR_030947
Natural varianti985 – 9851G → V in BFH. 1 Publication
VAR_030948
Natural varianti1015 – 10151G → E in BFH. 1 Publication
VAR_030949
Natural varianti1167 – 11671G → R in APSAD; in isolated microhematuria at heterozygosity. 1 Publication
VAR_011211
Natural varianti1207 – 12071G → E in APSAR; in isolated microhematuria at heterozygosity. 1 Publication
VAR_011212
Natural varianti1215 – 12151R → Q in APSAR; unknown pathological significance. 1 Publication
VAR_011213
Natural varianti1216 – 12161G → R in APSAR. 1 Publication
VAR_030950
Natural varianti1269 – 12691D → E.1 Publication
Corresponds to variant rs57611801 [ dbSNP | Ensembl ].
VAR_011214
Natural varianti1277 – 12771G → S in APSAR. 1 Publication
Corresponds to variant rs190598500 [ dbSNP | Ensembl ].
VAR_011215
Natural varianti1330 – 13301I → T in APSAR; unknown pathological significance. 1 Publication
VAR_011216
Natural varianti1334 – 13341G → E in APSAR. 1 Publication
VAR_011217
Natural varianti1347 – 13471D → E in APSAR; unknown pathological significance. 1 Publication
Corresponds to variant rs73996414 [ dbSNP | Ensembl ].
VAR_011218
Natural varianti1474 – 14741L → P.2 Publications
Corresponds to variant rs200302125 [ dbSNP | Ensembl ].
VAR_001908
Natural varianti1495 – 14951Q → R.
Corresponds to variant rs77964815 [ dbSNP | Ensembl ].
VAR_001909
Natural varianti1661 – 16611R → C in APSAR. 1 Publication
VAR_011219

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1418 – 14247GPAGSDG → ESLFHQL in isoform 5. 1 PublicationVSP_023498
Alternative sequencei1425 – 1670246Missing in isoform 5. 1 PublicationVSP_023499Add
BLAST
Alternative sequencei1488 – 1670183GTLGS…MKKRH → DALFVKVLRSP in isoform 3. 2 PublicationsVSP_001171Add
BLAST
Alternative sequencei1488 – 1670183GTLGS…MKKRH → ESLFHQL in isoform 4. 1 PublicationVSP_023500Add
BLAST
Alternative sequencei1586 – 167085FTSAG…MKKRH → KAYSINCESWGIRKNNKSLS GVHEEKTLKLKKTAELVFFI LKNKVMTEHAVI in isoform 2. 2 PublicationsVSP_001170Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80031 mRNA. Translation: CAA56335.1.
AJ288487
, AJ288488, AJ288489, AJ288490, AJ288491, AJ288492, AJ288493, AJ288494, AJ288495, AJ288496, AJ288497, AJ288498, AJ288499, AJ288500, AJ288501, AJ288502, AJ288503, AJ288504, AJ288505, AJ288506, AJ288507, AJ288508, AJ288509, AJ288510, AJ288511, AJ288512, AJ288513, AJ288514, AJ288515, AJ288516, AJ288517, AJ288518, AJ288519, AJ288520, AJ288521, AJ288522, AJ288523, AJ288524, AJ288525, AJ288526, AJ288527, AJ288528, AJ288529, AJ288530, AJ288531, AJ288532, AJ288533, AJ288534, AJ288535, AJ288536, AJ288537, AJ288538 Genomic DNA. Translation: CAC36101.1.
AC079235 Genomic DNA. Translation: AAY14671.1.
AC097662 Genomic DNA. Translation: AAY24251.1.
AC107069 Genomic DNA. Translation: AAX93111.1.
AB008496 Genomic DNA. Translation: BAA25064.1.
M81379 mRNA. Translation: AAA51556.1.
M92993 mRNA. Translation: AAA21610.1.
AF258351 mRNA. Translation: AAF72632.1.
U02519 mRNA. Translation: AAA18942.1.
U02520 mRNA. Translation: AAA18943.1.
S55790 mRNA. Translation: AAB19637.1.
L08650 Genomic DNA. Translation: AAA52044.1.
CCDSiCCDS42829.1. [Q01955-1]
PIRiA49736.
A54763. CGHU3B.
B49736.
S69113.
RefSeqiNP_000082.2. NM_000091.4. [Q01955-1]
UniGeneiHs.570065.

Genome annotation databases

EnsembliENST00000396578; ENSP00000379823; ENSG00000169031. [Q01955-1]
GeneIDi1285.
KEGGihsa:1285.
UCSCiuc002vom.2. human. [Q01955-1]

Polymorphism databases

DMDMi134035067.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80031 mRNA. Translation: CAA56335.1 .
AJ288487
, AJ288488 , AJ288489 , AJ288490 , AJ288491 , AJ288492 , AJ288493 , AJ288494 , AJ288495 , AJ288496 , AJ288497 , AJ288498 , AJ288499 , AJ288500 , AJ288501 , AJ288502 , AJ288503 , AJ288504 , AJ288505 , AJ288506 , AJ288507 , AJ288508 , AJ288509 , AJ288510 , AJ288511 , AJ288512 , AJ288513 , AJ288514 , AJ288515 , AJ288516 , AJ288517 , AJ288518 , AJ288519 , AJ288520 , AJ288521 , AJ288522 , AJ288523 , AJ288524 , AJ288525 , AJ288526 , AJ288527 , AJ288528 , AJ288529 , AJ288530 , AJ288531 , AJ288532 , AJ288533 , AJ288534 , AJ288535 , AJ288536 , AJ288537 , AJ288538 Genomic DNA. Translation: CAC36101.1 .
AC079235 Genomic DNA. Translation: AAY14671.1 .
AC097662 Genomic DNA. Translation: AAY24251.1 .
AC107069 Genomic DNA. Translation: AAX93111.1 .
AB008496 Genomic DNA. Translation: BAA25064.1 .
M81379 mRNA. Translation: AAA51556.1 .
M92993 mRNA. Translation: AAA21610.1 .
AF258351 mRNA. Translation: AAF72632.1 .
U02519 mRNA. Translation: AAA18942.1 .
U02520 mRNA. Translation: AAA18943.1 .
S55790 mRNA. Translation: AAB19637.1 .
L08650 Genomic DNA. Translation: AAA52044.1 .
CCDSi CCDS42829.1. [Q01955-1 ]
PIRi A49736.
A54763. CGHU3B.
B49736.
S69113.
RefSeqi NP_000082.2. NM_000091.4. [Q01955-1 ]
UniGenei Hs.570065.

3D structure databases

ProteinModelPortali Q01955.
SMRi Q01955. Positions 1445-1668.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107682. 3 interactions.
IntActi Q01955. 1 interaction.
STRINGi 9606.ENSP00000379823.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei Q01955.

Polymorphism databases

DMDMi 134035067.

Proteomic databases

MaxQBi Q01955.
PaxDbi Q01955.
PRIDEi Q01955.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000396578 ; ENSP00000379823 ; ENSG00000169031 . [Q01955-1 ]
GeneIDi 1285.
KEGGi hsa:1285.
UCSCi uc002vom.2. human. [Q01955-1 ]

Organism-specific databases

CTDi 1285.
GeneCardsi GC02P227993.
GeneReviewsi COL4A3.
H-InvDB HIX0002893.
HIX0029836.
HGNCi HGNC:2204. COL4A3.
HPAi HPA042064.
MIMi 104200. phenotype.
120070. gene.
141200. phenotype.
203780. phenotype.
neXtProti NX_Q01955.
Orphaneti 88918. Autosomal dominant Alport syndrome.
88919. Autosomal recessive Alport syndrome.
97562. Benign familial hematuria.
PharmGKBi PA26719.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120455.
HOVERGENi HBG004933.
InParanoidi Q01955.
KOi K06237.
OMAi SPGCPGK.
OrthoDBi EOG7RZ5P3.
PhylomeDBi Q01955.
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

GeneWikii Collagen_alpha-3(IV)_chain.
GenomeRNAii 1285.
NextBioi 5191.
PROi Q01955.
SOURCEi Search...

Gene expression databases

Bgeei Q01955.
CleanExi HS_COL4A3.
ExpressionAtlasi Q01955. baseline and differential.
Genevestigatori Q01955.

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. 22 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 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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS PRO-141; GLY-162 AND LEU-574.
    Tissue: Kidney.
  2. Leinonen A.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Structure of the human type IV collagen gene COL4A3 and mutations in autosomal Alport syndrome."
    Heidet L., Arrondel C., Forestier L., Cohen-Solal L., Mollet G., Gutierrez B., Stavrou C., Gubler M.-C., Antignac C.
    J. Am. Soc. Nephrol. 12:97-106(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS APSAR GLU-297; ARG-407; ARG-640; GLU-1207; GLN-1215; SER-1277; THR-1330; GLU-1334; GLU-1347 AND CYS-1661, VARIANT APSAD ARG-1167, VARIANTS ARG-43; PRO-141; TYR-326; HIS-408; ARG-451; GLU-1269 AND PRO-1474.
  4. "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].
  5. "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 1-29.
  6. "Molecular cloning of the human Goodpasture antigen demonstrates it to be the alpha 3 chain of type IV collagen."
    Turner N., Mason P.J., Brown R., Fox M., Povey S., Rees A., Pusey C.D.
    J. Clin. Invest. 89:592-601(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1331-1670 (ISOFORM 1).
    Tissue: Kidney.
  7. "Exon/intron structure of the human alpha 3(IV) gene encompassing the Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially antigenic region at the triple helix/NC1 domain junction."
    Quinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.
    J. Biol. Chem. 267:19780-19784(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1670 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  8. Erratum
    Quinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.
    J. Biol. Chem. 269:17358-17358(1994) [PubMed] [Europe PMC] [Abstract]
  9. "Characterization and expression of multiple alternatively spliced transcripts of the Goodpasture antigen gene region. Goodpasture antibodies recognize recombinant proteins representing the autoantigen and one of its alternative forms."
    Penades J.R., Bernal D., Revert F., Johansson C., Fresquet V.J., Cervera J., Wieslander J., Quinones S., Saus J.
    Eur. J. Biochem. 229:754-760(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1670 (ISOFORMS 1; 2; 3; 4 AND 5), ALTERNATIVE SPLICING.
    Tissue: Kidney.
  10. "Distinct antitumor properties of a type IV collagen domain derived from basement membrane."
    Maeshima Y., Colorado P.C., Torre A., Holthaus K.A., Grunkemeyer J.A., Ericksen M.B., Hopfer H., Xiao Y., Stillman I.E., Kalluri R.
    J. Biol. Chem. 275:21340-21348(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1426-1670 (ISOFORM 1), FUNCTION.
  11. "Alternative splicing of the NC1 domain of the human alpha 3(IV) collagen gene. Differential expression of mRNA transcripts that predict three protein variants with distinct carboxyl regions."
    Feng L., Xia Y., Wilson C.B.
    J. Biol. Chem. 269:2342-2348(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1439-1670 (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING (ISOFORM 1).
    Tissue: Kidney.
  12. "Sequence and localization of a partial cDNA encoding the human alpha 3 chain of type IV collagen."
    Morrison K.E., Mariyama M., Yang-Feng T.L., Reeders S.T.
    Am. J. Hum. Genet. 49:545-554(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1453-1670 (ISOFORM 1).
  13. Ding J.
    Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1644-1670 (ISOFORM 1).
    Tissue: Kidney.
  14. "The human mRNA encoding the Goodpasture antigen is alternatively spliced."
    Bernal D., Quinones S., Saus J.
    J. Biol. Chem. 268:12090-12094(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Kidney.
  15. "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: TISSUE SPECIFICITY.
  16. "Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen."
    Raya A., Revert F., Navarro S., Saus J.
    J. Biol. Chem. 274:12642-12649(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COL4A3BP, PHOSPHORYLATION.
  17. "Two RGD-independent alpha vbeta 3 integrin binding sites on tumstatin regulate distinct anti-tumor properties."
    Maeshima Y., Colorado P.C., Kalluri R.
    J. Biol. Chem. 275:23745-23750(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: INVOLVEMENT IN APSAD.
  19. "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.
  20. "Human tumstatin and human endostatin exhibit distinct antiangiogenic activities mediated by alpha v beta 3 and alpha 5 beta 1 integrins."
    Sudhakar A., Sugimoto H., Yang C., Lively J., Zeisberg M., Kalluri R.
    Proc. Natl. Acad. Sci. U.S.A. 100:4766-4771(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ITGB3.
  21. "Implication of tumstatin in tumor progression of human bronchopulmonary carcinomas."
    Caudroy S., Cucherousset J., Lorenzato M., Zahm J.-M., Martinella-Catusse C., Polette M., Birembaut P.
    Hum. Pathol. 35:1218-1222(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1414.
    Tissue: Mammary cancer.
  23. Cited for: VARIANT PRO-1474.
  24. "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: VARIANTS BFH VAL-985 AND GLU-1015.
  25. "Novel COL4A5, COL4A4, and COL4A3 mutations in Alport syndrome."
    Nagel M., Nagorka S., Gross O.
    Hum. Mutat. 26:60-60(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS APSAR ASP-532; ARG-739; ARG-853 AND ARG-1216.

Entry informationi

Entry nameiCO4A3_HUMAN
AccessioniPrimary (citable) accession number: Q01955
Secondary accession number(s): Q53QQ1
, Q53R14, Q53RW8, Q9BQT2, Q9NYC4, Q9UDJ9, Q9UDK9, Q9UDL0, Q9UDL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 6, 2007
Last modified: November 26, 2014
This is version 173 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

Miscellaneous

The epitopes recognized by the Goodpasture autoantibodies are sequestered within the NC1 hexamer of the type IV collagen network.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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