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P29400 (CO4A5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-5(IV) chain
Gene names
Name:COL4A5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane.

Tissue specificity

Isoform 2 is found in kidney.

Domain

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.

Post-translational modification

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.

Involvement in disease

Alport syndrome, X-linked (APSX) [MIM:301050]: A syndrome that is characterized by progressive glomerulonephritis, renal failure, sensorineural deafness, specific eye abnormalities (lenticonous and macular flecks), and glomerular basement membrane defects. The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Deletions covering the N-terminal regions of COL4A5 and COL4A6, which are localized in a head-to-head manner, are found in the chromosome Xq22.3 centromeric deletion syndrome. This results in a phenotype with features of diffuse leiomyomatosis and Alport syndrome (DL-ATS). Ref.17 Ref.33

Sequence similarities

Belongs to the type IV collagen family.

Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29400-1)

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.
Isoform 2 (identifier: P29400-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1264-1264: G → GPTGFQG
Note: Contains 2 extra G-X-X repeats into the triple-helix domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 16851659Collagen alpha-5(IV) chain
PRO_0000005852

Regions

Domain1461 – 1685225Collagen IV NC1
Region27 – 4115Nonhelical region (NC2)
Region42 – 14561415Triple-helical region

Amino acid modifications

Glycosylation1251N-linked (GlcNAc...) Potential
Disulfide bond451Interchain Potential
Disulfide bond481Interchain Potential
Disulfide bond484Interchain Potential
Disulfide bond1476 ↔ 1567Or C-1476 with C-1564 By similarity
Disulfide bond1509 ↔ 1564Or C-1509 with C-1567 By similarity
Disulfide bond1521 ↔ 1527 By similarity
Disulfide bond1586 ↔ 1681Or C-1586 with C-1678 By similarity
Disulfide bond1620 ↔ 1678Or C-1620 with C-1681 By similarity
Disulfide bond1632 ↔ 1638 By similarity
Cross-link1549S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1667) By similarity
Cross-link1667S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1549) By similarity

Natural variations

Alternative sequence12641G → GPTGFQG in isoform 2.
VSP_001173
Natural variant541G → D in APSX; adult type.
VAR_001914
Natural variant1141G → S in APSX.
VAR_007991
Natural variant1291G → E in APSX; juvenile type.
VAR_001915
Natural variant1291G → V in APSX; juvenile type.
VAR_001916
Natural variant1741G → R in APSX. Ref.24
VAR_001917
Natural variant1771G → C in APSX; presenting with dot-and-fleck retinopathy. Ref.29
VAR_011220
Natural variant1771G → R in APSX; adult type. Ref.24
VAR_001918
Natural variant1921G → R in APSX. Ref.32
VAR_011221
Natural variant2041G → V in APSX; juvenile type.
VAR_011222
Natural variant2161G → R in APSX; juvenile type. Ref.30
VAR_001919
Natural variant2191G → S in APSX.
VAR_001920
Natural variant2301G → R in APSX; juvenile type.
VAR_011223
Natural variant2391G → E in APSX.
VAR_011224
Natural variant2641G → R in APSX; adult type.
VAR_011225
Natural variant2891G → V in APSX; juvenile type.
VAR_001921
Natural variant2921G → R in APSX. Ref.32
VAR_011226
Natural variant2921G → V in APSX; juvenile type.
VAR_001922
Natural variant2951G → D in APSX. Ref.32
VAR_011227
Natural variant2981G → S in APSX.
VAR_011228
Natural variant3191G → R in APSX; juvenile type. Ref.31
VAR_011229
Natural variant3251G → E in APSX. Ref.15
VAR_001923
Natural variant3251G → R in APSX; juvenile and adult types. Ref.14 Ref.24 Ref.32
VAR_001924
Natural variant3311G → V in APSX.
VAR_007992
Natural variant365 – 3673Missing in APSX; juvenile type.
VAR_001926
Natural variant3651G → E in APSX; juvenile type.
VAR_001925
Natural variant3711G → E in APSX; juvenile type.
VAR_001927
Natural variant3741G → A in APSX.
VAR_001928
Natural variant3831G → D in APSX; juvenile type.
VAR_001929
Natural variant4001G → E in APSX; adult type. Ref.18
VAR_001930
Natural variant4061G → V in APSX; adult type. Ref.18
VAR_001931
Natural variant4091G → D in APSX.
VAR_001932
Natural variant4121G → V in APSX; adult type.
VAR_011230
Natural variant4151G → R in APSX. Ref.30
VAR_011231
Natural variant4201G → E in APSX; juvenile type.
VAR_011232
Natural variant4201G → V in APSX. Ref.25
VAR_011233
Natural variant4231G → E in APSX.
VAR_011234
Natural variant4301A → D. Ref.21
Corresponds to variant rs142883891 [ dbSNP | Ensembl ].
VAR_001933
Natural variant4441I → S. Ref.21 Ref.26 Ref.32
Corresponds to variant rs2272946 [ dbSNP | Ensembl ].
VAR_001934
Natural variant456 – 4583Missing in APSX.
VAR_001935
Natural variant4661G → E in APSX.
VAR_001936
Natural variant4721G → R in APSX.
VAR_007993
Natural variant4911G → E in APSX; juvenile type.
VAR_011235
Natural variant4941G → D in APSX; adult type.
VAR_001937
Natural variant496 – 50712Missing in APSX; juvenile type.
VAR_001938
Natural variant4971G → C in APSX; adult type.
VAR_011236
Natural variant5211G → C in APSX. Ref.4
VAR_001939
Natural variant5211G → S in APSX.
VAR_001940
Natural variant5241G → D in APSX; adult type.
VAR_011237
Natural variant5451G → R in APSX.
VAR_007994
Natural variant5451G → V in APSX.
VAR_007995
Natural variant5581G → R in APSX. Ref.32
VAR_011238
Natural variant5611G → R in APSX.
VAR_007996
Natural variant5671G → A in APSX; juvenile type.
VAR_001941
Natural variant5731G → D in APSX. Ref.25
VAR_011239
Natural variant5791G → E in APSX. Ref.26
VAR_011240
Natural variant5791G → R in APSX; adult type.
VAR_007997
Natural variant6031G → V in APSX. Ref.32
VAR_011241
Natural variant6091G → R in APSX; juvenile type.
VAR_011242
Natural variant6091G → V in APSX; juvenile type.
VAR_001942
Natural variant6191P → S. Ref.21
VAR_011243
Natural variant6211G → C in APSX.
VAR_011244
Natural variant6241G → D in APSX. Ref.25 Ref.32
VAR_011245
Natural variant6291G → D in APSX. Ref.32
VAR_011246
Natural variant6321G → D in APSX.
VAR_011247
Natural variant6331E → K in APSX. Ref.26
VAR_011248
Natural variant6351G → D in APSX. Ref.25
VAR_007998
Natural variant6381G → A in APSX. Ref.18
VAR_001944
Natural variant6381G → S in APSX; juvenile type.
VAR_007999
Natural variant6381G → V in APSX. Ref.18
VAR_001943
Natural variant6531G → R in APSX; juvenile type. Ref.18
VAR_001945
Natural variant6641K → N. Ref.21
Corresponds to variant rs34077552 [ dbSNP | Ensembl ].
VAR_001946
Natural variant6691G → A in APSX; juvenile type.
VAR_008000
Natural variant6811G → D in APSX.
VAR_011249
Natural variant6841G → V in APSX; adult type.
VAR_001947
Natural variant6871G → E in APSX.
VAR_008001
Natural variant7221G → E in APSX. Ref.32
VAR_011250
Natural variant7391P → A. Ref.26
Corresponds to variant rs104886164 [ dbSNP | Ensembl ].
VAR_011251
Natural variant7391P → S in APSX; juvenile type. Ref.31
Corresponds to variant rs104886164 [ dbSNP | Ensembl ].
VAR_011252
Natural variant7401G → E in APSX; juvenile type.
VAR_001948
Natural variant7431G → D in APSX.
VAR_008002
Natural variant7721G → D in APSX; juvenile type.
VAR_001949
Natural variant7961G → R in APSX. Ref.18
VAR_001950
Natural variant802 – 8076Missing in APSX.
VAR_011254
Natural variant8021G → R in APSX.
VAR_011253
Natural variant8081G → E in APSX; adult type.
VAR_008003
Natural variant8111G → V in APSX; juvenile type.
VAR_011255
Natural variant822 – 8243Missing in APSX.
VAR_008004
Natural variant8221G → R in APSX. Ref.27
VAR_011256
Natural variant8521G → E in APSX; juvenile type.
VAR_008005
Natural variant8521G → R in APSX.
VAR_001951
Natural variant864 – 87512Missing in APSX.
VAR_011257
Natural variant8661G → E in APSX; adult type.
VAR_001952
Natural variant8691G → R in APSX; juvenile type. Ref.18 Ref.25
VAR_001953
Natural variant8721G → R in APSX. Ref.18
VAR_001954
Natural variant8781G → R in APSX.
VAR_008006
Natural variant8981M → V in APSX; mild phenotype. Ref.32
VAR_011258
Natural variant9021G → V in APSX; juvenile type. Ref.31
VAR_011259
Natural variant9111G → E in APSX. Ref.31
VAR_011260
Natural variant9411G → C in APSX. Ref.25
VAR_011261
Natural variant9421Missing in APSX.
VAR_001955
Natural variant9471G → D in APSX. Ref.26
VAR_011262
Natural variant9531G → V in APSX; found on the same allele as variant Glu-1211. Ref.26
Corresponds to variant rs78972735 [ dbSNP | Ensembl ].
VAR_011263
Natural variant988 – 9925Missing in APSX; adult type.
VAR_008007
Natural variant10061G → A in APSX. Ref.32
VAR_011264
Natural variant10061G → V in APSX. Ref.32
VAR_011265
Natural variant10151G → E in APSX.
VAR_011266
Natural variant10151G → V in APSX.
VAR_011267
Natural variant10301G → S in APSX. Ref.25
VAR_011268
Natural variant10361G → V in APSX.
VAR_011269
Natural variant10391G → S in APSX; juvenile type.
VAR_011270
Natural variant10451G → E in APSX. Ref.30
VAR_011271
Natural variant10661G → R in APSX.
VAR_011272
Natural variant10661G → S in APSX. Ref.25
VAR_011273
Natural variant10861G → D in APSX. Ref.30
VAR_011274
Natural variant11041G → V in APSX.
VAR_001956
Natural variant11071G → R in APSX. Ref.26
VAR_008008
Natural variant11431G → D in APSX; juvenile type. Ref.25
VAR_001957
Natural variant11431G → S in APSX; adult type.
VAR_001958
Natural variant11581G → R in APSX. Ref.26
VAR_011275
Natural variant11611G → R in APSX.
VAR_008009
Natural variant11671G → S in APSX. Ref.30
VAR_011276
Natural variant11701G → S in APSX. Ref.26
VAR_011277
Natural variant11821G → R in APSX; juvenile type.
VAR_001959
Natural variant11961G → R in APSX. Ref.25
VAR_011278
Natural variant12051G → C in APSX; juvenile type.
VAR_011279
Natural variant12111G → E in APSX; found on the same allele as variant Val-953.
VAR_011280
Natural variant12111G → R in APSX.
VAR_008010
Natural variant12201G → D in APSX.
VAR_008011
Natural variant12291G → D in APSX; adult type. Ref.31
VAR_011281
Natural variant12411G → C in APSX. Ref.18
VAR_001960
Natural variant12441G → D in APSX. Ref.32
VAR_011282
Natural variant12521G → S in APSX; adult type.
VAR_011283
Natural variant12611G → E in APSX. Ref.25
VAR_011284
Natural variant12701G → S in APSX.
VAR_001961
Natural variant13331G → S in APSX.
VAR_008012
Natural variant13571G → S in APSX. Ref.25
VAR_011285
Natural variant13791G → V in APSX; adult type.
VAR_001962
Natural variant14101R → C in APSX; adult and juvenile types. Ref.24
VAR_001963
Natural variant14211G → W in APSX; adult type. Ref.24
VAR_001964
Natural variant14221R → C in APSX; juvenile type.
VAR_001965
Natural variant14271G → V in APSX; adult type.
VAR_008013
Natural variant14281L → M. Ref.21
VAR_011286
Natural variant14421G → D in APSX.
VAR_008014
Natural variant14511G → S in APSX.
VAR_001966
Natural variant14861G → A in APSX; adult type.
VAR_008015
Natural variant14881S → F in APSX.
VAR_011287
Natural variant14981A → D in APSX. Ref.22
VAR_001967
Natural variant15111R → H in APSX; juvenile type; could be a non pathogenic variant. Ref.31
VAR_011288
Natural variant15171P → T in APSX; juvenile type. Ref.16 Ref.24
VAR_001968
Natural variant15381W → S in APSX; adult type. Ref.16
VAR_001969
Natural variant15591P → A.
VAR_008016
Natural variant15631R → Q in APSX. Ref.16
VAR_001970
Natural variant15641C → S in APSX; adult type. Ref.13
VAR_001971
Natural variant15671C → R in APSX; juvenile type.
VAR_011289
Natural variant15961G → D in APSX. Ref.24
VAR_001972
Natural variant1597 – 168589Missing in APSX.
VAR_019594
Natural variant16491L → R in APSX; adult type. Ref.19 Ref.25 Ref.32
VAR_001973
Natural variant16771R → P in APSX. Ref.32
VAR_011290
Natural variant16771R → Q in APSX. Ref.23
VAR_001974
Natural variant16781C → W in APSX. Ref.26
VAR_011291
Natural variant1679 – 16857Missing in APSX.
VAR_019595

Experimental info

Sequence conflict440 – 4412AG → GS in AAA99480. Ref.5
Sequence conflict625 – 6284FGPP → LALQ in AAA99480. Ref.5
Sequence conflict667 – 6682LP → FR in AAA99480. Ref.5
Sequence conflict8881A → R in AAA99480. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 4450A6762F12A626

FASTA1,685161,044
        10         20         30         40         50         60 
MKLRGVSLAA GLFLLALSLW GQPAEAAACY GCSPGSKCDC SGIKGEKGER GFPGLEGHPG 

        70         80         90        100        110        120 
LPGFPGPEGP PGPRGQKGDD GIPGPPGPKG IRGPPGLPGF PGTPGLPGMP GHDGAPGPQG 

       130        140        150        160        170        180 
IPGCNGTKGE RGFPGSPGFP GLQGPPGPPG IPGMKGEPGS IIMSSLPGPK GNPGYPGPPG 

       190        200        210        220        230        240 
IQGLPGPTGI PGPIGPPGPP GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP 

       250        260        270        280        290        300 
PGQISEQKRP IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGEKGEKGE QGEPGKRGKP 

       310        320        330        340        350        360 
GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDTGPPG PPGLVIPRPG TGITIGEKGN 

       370        380        390        400        410        420 
IGLPGLPGEK GERGFPGIQG PPGLPGPPGA AVMGPPGPPG FPGERGQKGD EGPPGISIPG 

       430        440        450        460        470        480 
PPGLDGQPGA PGLPGPPGPA GPHIPPSDEI CEPGPPGPPG SPGDKGLQGE QGVKGDKGDT 

       490        500        510        520        530        540 
CFNCIGTGIS GPPGQPGLPG LPGPPGSLGF PGQKGEKGQA GATGPKGLPG IPGAPGAPGF 

       550        560        570        580        590        600 
PGSKGEPGDI LTFPGMKGDK GELGSPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGITFKG 

       610        620        630        640        650        660 
ERGPPGNPGL PGLPGNIGPM GPPGFGPPGP VGEKGIQGVA GNPGQPGIPG PKGDPGQTIT 

       670        680        690        700        710        720 
QPGKPGLPGN PGRDGDVGLP GDPGLPGQPG LPGIPGSKGE PGIPGIGLPG PPGPKGFPGI 

       730        740        750        760        770        780 
PGPPGAPGTP GRIGLEGPPG PPGFPGPKGE PGFALPGPPG PPGLPGFKGA LGPKGDRGFP 

       790        800        810        820        830        840 
GPPGPPGRTG LDGLPGPKGD VGPNGQPGPM GPPGLPGIGV QGPPGPPGIP GPIGQPGLHG 

       850        860        870        880        890        900 
IPGEKGDPGP PGLDVPGPPG ERGSPGIPGA PGPIGPPGSP GLPGKAGASG FPGTKGEMGM 

       910        920        930        940        950        960 
MGPPGPPGPL GIPGRSGVPG LKGDDGLQGQ PGLPGPTGEK GSKGEPGLPG PPGPMDPNLL 

       970        980        990       1000       1010       1020 
GSKGEKGEPG LPGIPGVSGP KGYQGLPGDP GQPGLSGQPG LPGPPGPKGN PGLPGQPGLI 

      1030       1040       1050       1060       1070       1080 
GPPGLKGTIG DMGFPGPQGV EGPPGPSGVP GQPGSPGLPG QKGDKGDPGI SSIGLPGLPG 

      1090       1100       1110       1120       1130       1140 
PKGEPGLPGY PGNPGIKGSV GDPGLPGLPG TPGAKGQPGL PGFPGTPGPP GPKGISGPPG 

      1150       1160       1170       1180       1190       1200 
NPGLPGEPGP VGGGGHPGQP GPPGEKGKPG QDGIPGPAGQ KGEPGQPGFG NPGPPGLPGL 

      1210       1220       1230       1240       1250       1260 
SGQKGDGGLP GIPGNPGLPG PKGEPGFHGF PGVQGPPGPP GSPGPALEGP KGNPGPQGPP 

      1270       1280       1290       1300       1310       1320 
GRPGLPGPEG PPGLPGNGGI KGEKGNPGQP GLPGLPGLKG DQGPPGLQGN PGRPGLNGMK 

      1330       1340       1350       1360       1370       1380 
GDPGLPGVPG FPGMKGPSGV PGSAGPEGEP GLIGPPGPPG LPGPSGQSII IKGDAGPPGI 

      1390       1400       1410       1420       1430       1440 
PGQPGLKGLP GPQGPQGLPG PTGPPGDPGR NGLPGFDGAG GRKGDPGLPG QPGTRGLDGP 

      1450       1460       1470       1480       1490       1500 
PGPDGLQGPP GPPGTSSVAH GFLITRHSQT TDAPQCPQGT LQVYEGFSLL YVQGNKRAHG 

      1510       1520       1530       1540       1550       1560 
QDLGTAGSCL RRFSTMPFMF CNINNVCNFA SRNDYSYWLS TPEPMPMSMQ PLKGQSIQPF 

      1570       1580       1590       1600       1610       1620 
ISRCAVCEAP AVVIAVHSQT IQIPHCPQGW DSLWIGYSFM MHTSAGAEGS GQALASPGSC 

      1630       1640       1650       1660       1670       1680 
LEEFRSAPFI ECHGRGTCNY YANSYSFWLA TVDVSDMFSK PQSETLKAGD LRTRISRCQV 


CMKRT 

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Isoform 2 [UniParc].

Checksum: E45612A1C153D123
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FASTA1,691161,632

References

« Hide 'large scale' references
[1]"Structure of the human type IV collagen COL4A5 gene."
Zhou J., Leinonen A., Tryggvason K.
J. Biol. Chem. 269:6608-6614(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Complete amino acid sequence of the human alpha 5 (IV) collagen chain and identification of a single-base mutation in exon 23 converting glycine 521 in the collagenous domain to cysteine in an Alport syndrome patient."
Zhou J., Hertz J.M., Leinonen A., Tryggvason K.
J. Biol. Chem. 267:12475-12481(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-910, VARIANT APSX CYS-521.
Tissue: Kidney.
[5]"Complete primary structure of the triple-helical region and the carboxyl-terminal domain of a new type IV collagen chain, alpha 5(IV)."
Pihlajaniemi T., Pohjolainen E.R., Myers J.C.
J. Biol. Chem. 265:13758-13766(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-1685.
Tissue: Placenta.
[6]"Characterization of the 3' half of the human type IV collagen alpha 5 gene that is affected in the Alport syndrome."
Zhou J., Hostikka S.L., Chow L.T., Tryggvason K.
Genomics 9:1-9(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 924-1685.
[7]"Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome."
Hostikka S.L., Eddy R.L., Byers M.G., Hoeyhtyae M., Shows T.B., Tryggvason K.
Proc. Natl. Acad. Sci. U.S.A. 87:1606-1610(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 914-1685.
[8]"Molecular cloning of alpha 5(IV) collagen and assignment of the gene to the region of the X chromosome containing the Alport syndrome locus."
Myers J.C., Jones T.A., Pohjolainen E.R., Kadri A.S., Goddard A.D., Sheer D., Solomon E., Pihlajaniemi T.
Am. J. Hum. Genet. 46:1024-1033(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1442-1471.
[9]Guo C., van Damme B., Vanrenterghem Y., Devriendt K., Cassiman J.-J., Marynen P.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-20.
[10]"Differential splicing of COL4A5 mRNA in kidney and white blood cells: a complex mutation in the COL4A5 gene of an Alport patient deletes the NC1 domain."
Guo C., van Damme B., van Damme-Lombaerts R., van den Berghe H., Cassiman J.-J., Marynen P.
Kidney Int. 44:1316-1321(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1258-1270 (ISOFORM 2).
[11]"Mutations in the COL4A5 gene in Alport syndrome: a possible mutation in primordial germ cells."
Nakazato H., Hattori S., Ushijima T., Matsuura T., Koitabashi Y., Takada T., Yoshioka K., Endo F., Matsuda I.
Kidney Int. 46:1307-1314(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1589-1598 AND 1677-1685, VARIANTS APSX 1597-TYR--THR-1685 DEL AND 1679-GLQ--THR-1685 DEL.
[12]"The clinical spectrum of type IV collagen mutations."
Lemmink H.H., Schroeder C.H., Monnens L.A.H., Smeets H.J.M.
Hum. Mutat. 9:477-499(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[13]"Single base mutation in alpha 5(IV) collagen chain gene converting a conserved cysteine to serine in Alport syndrome."
Zhou J., Barker D.F., Hostikka S.L., Gregory M.C., Atkin C.L., Tryggvason K.
Genomics 9:10-18(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX SER-1564.
[14]"Substitution of arginine for glycine 325 in the collagen alpha 5 (IV) chain associated with X-linked Alport syndrome: characterization of the mutation by direct sequencing of PCR-amplified lymphoblast cDNA fragments."
Knebelmann B., Deschenes G., Gros F., Hors M.-C., Gruenfeld J.-P., Tryggvason K., Gubler M.-C., Antignac C.
Am. J. Hum. Genet. 51:135-142(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX ARG-325.
[15]"De novo mutation in the COL4A5 gene converting glycine 325 to glutamic acid in Alport syndrome."
Renieri A., Seri M., Myers J.C., Pihlajaniemi T., Massella L., Rizzoni G.F., de Marchi M.
Hum. Mol. Genet. 1:127-129(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX GLU-325.
[16]"Identification of four novel mutations in the COL4A5 gene of patients with Alport syndrome."
Lemmink H.L., Schroeder C.H., Brunner H.G., Nelen M.R., Zhou J., Tryggvason K., Haggsma-Schouten W.A.G., Roodvoets A.P., Rascher W., van Oost B.A., Smeets H.J.M.
Genomics 17:485-489(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX THR-1517; SER-1538 AND GLN-1563.
[17]"Deletion of the paired alpha 5(IV) and alpha 6(IV) collagen genes in inherited smooth muscle tumors."
Zhou J., Mochizuki T., Smeets H., Antignac C., Laurila P., de Paepe A., Tryggvason K., Reeders S.T.
Science 261:1167-1169(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DL-ATS.
[18]"Detection of 12 novel mutations in the collagenous domain of the COL4A5 gene in Alport syndrome patients."
Boye E., Flinter F., Zhou J., Tryggvason K., Bobrow M., Harris A.
Hum. Mutat. 5:197-204(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX GLU-400; VAL-406; VAL-638; ALA-638; ARG-653; ARG-796; ARG-869; ARG-872 AND CYS-1241.
[19]"A mutation causing Alport syndrome with tardive hearing loss is common in the western United States."
Barker D.F., Pruchno C.J., Jiang X., Atkin C.L., Stone E.M., Denison J.C., Fain P.R., Gregory M.C.
Am. J. Hum. Genet. 58:1157-1165(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX ARG-1649.
[20]"X-linked Alport syndrome: an SSCP-based mutation survey over all 51 exons of the COL4A5 gene."
Renieri A., Bruttini M., Galli L., Zanelli P., Neri T.M., Rossetti S., Turco A.E., Heiskari N., Zhou J., Gusmano R., Massella L., Banfi G., Scolari F., Sessa A., Rizzoni G.F., Tryggvason K., Pignatti P.F., Savi M., Ballabio A., de Marchi M.
Am. J. Hum. Genet. 58:1192-1204(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX.
[21]"Spectrum of mutations in the COL4A5 collagen gene in X-linked Alport syndrome."
Knebelmann B., Breillat C., Forestier L., Arrondel C., Jacassier D., Giatras I., Drouot L., Deschenes G., Gruenfeld J.-P., Broyer M., Gubler M.-C., Antignac C.
Am. J. Hum. Genet. 59:1221-1232(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX, VARIANTS ASP-430; SER-444; SER-619; ASN-664 AND MET-1428.
[22]"Substitution of A1498D in noncollagen domain of a5(IV) collagen chain associated with adult-onset X-linked Alport syndrome."
Tverskaya S., Bobrynina V., Tsalykova F., Ignatova M., Krasnopolskaya X., Evgrafov O.
Hum. Mutat. 7:149-150(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX ASP-1498.
[23]"Common ancestry of three Ashkenazi-American families with Alport syndrome and COL4A5 R1677Q."
Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.
Hum. Genet. 99:681-684(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX GLN-1677.
[24]"Missense mutations in the COL4A5 gene in patients with X-linked Alport syndrome."
Neri T.M., Zanelli P., de Palma G., Savi M., Rossetti S., Turco A.E., Pignatti G.F., Galli L., Bruttini M., Renieri A., Mingarelli R., Trivelli A., Pinciaroli A.R., Ragaiolo M., Rizzoni G.F., de Marchi M.
Hum. Mutat. Suppl. 1:S106-S109(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX ARG-174; ARG-177; ARG-325; CYS-1410; TRP-1421; THR-1517 AND ASP-1596.
[25]"High mutation detection rate in the COL4A5 collagen gene in suspected Alport syndrome using PCR and direct DNA sequencing."
Martin P., Heiskari N., Zhou J., Leinonen A., Tumelius T., Hertz J.M., Barker D.F., Gregory M.C., Atkin C.L., Styrkarsdottir U., Neumann H., Springate J., Shows T.B., Pettersson E., Tryggvason K.
J. Am. Soc. Nephrol. 9:2291-2301(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX VAL-420; 456-PRO--PRO-458 DEL; ASP-573; ASP-624; ASP-635; 802-GLY--PRO-807 DEL; ARG-869; CYS-941; SER-1030; SER-1066; ASP-1143; ARG-1196; GLU-1261; SER-1357 AND ARG-1649.
[26]"Detection of mutations in the COL4A5 gene in over 90% of male patients with X-linked Alport's syndrome by RT-PCR and direct sequencing."
Inoue Y., Nishio H., Shirakawa T., Nakanishi K., Nakamura H., Sumino K., Nishiyama K., Iijima K., Yoshikawa N.
Am. J. Kidney Dis. 34:854-862(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX GLU-579; LYS-633; ASP-947; VAL-953; ARG-1107; ARG-1158; SER-1170 AND TRP-1678, VARIANTS SER-444 AND ALA-739.
[27]"Three novel mutations in the COL4A5 gene in Mexican Alport syndrome patients."
Cruz-Robles D., Garcia-Torres R., Antignac C., Forestier L., Garcia de la Puente S., Correa-Rotter R., Garcia-Lopez E., Orozco L.
Clin. Genet. 56:242-243(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX ARG-822.
[28]"Detection of mutations in COL4A5 in patients with Alport syndrome."
Plant K.E., Green P.M., Vetrie D., Flinter F.A.
Hum. Mutat. 13:124-132(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX, VARIANTS.
[29]"Dot-and-fleck retinopathy in Alport syndrome caused by a novel mutation in the COL4A5 gene."
Blasi M.A., Rinaldi R., Renieri A., Petrucci R., De Bernardo C., Bruttini M., Grammatico P.
Am. J. Ophthalmol. 130:130-131(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSX CYS-177.
[30]"Spectrum of COL4A5 mutations in Finnish Alport syndrome patients."
Martin P., Heiskari N., Pajari H., Groenhagen-Riska C., Kaeaeriaeinen H., Koskimies O., Tryggvason K.
Hum. Mutat. 15:579-579(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX ARG-216; ARG-415; GLU-1045; ASP-1086; SER-1167 AND 864-SER--GLY-875 DEL.
[31]"Mutational analysis of COL4A5 gene in Korean Alport syndrome."
Cheong H.I., Park H.W., Ha I.S., Choi Y.
Pediatr. Nephrol. 14:117-121(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX ARG-319; SER-739; VAL-902; GLU-911; ASP-1229 AND HIS-1511.
[32]"Efficient detection of Alport syndrome COL4A5 mutations with multiplex genomic PCR-SSCP."
Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.
Am. J. Med. Genet. 98:148-160(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APSX ARG-192; ARG-292; ASP-295; ARG-325; ARG-558; VAL-603; ASP-624; ASP-629; GLU-722; VAL-898; ALA-1006; VAL-1006; ASP-1244; ARG-1649 AND PRO-1677, VARIANT SER-444.
[33]"Alport syndrome with diffuse leiomyomatosis."
Anker M.C., Arnemann J., Neumann K., Ahrens P., Schmidt H., Koenig R.
Am. J. Med. Genet. A 119:381-385(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DL-ATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58526 mRNA. Translation: AAA99480.1.
AL034369, AL031622, AL035425 Genomic DNA. Translation: CAA22267.2.
AL035425, AL031622, AL034369 Genomic DNA. Translation: CAB90289.2.
AL031622, AL034369, AL035425 Genomic DNA. Translation: CAI43038.1.
AL136364 Genomic DNA. No translation available.
CH471120 Genomic DNA. Translation: EAX02683.1.
M90464 mRNA. Translation: AAA52046.1.
U04520 expand/collapse EMBL AC list , U04470, U04471, U04472, U04473, U04474, U04476, U04477, U04478, U04479, U04480, U04483, U04485, U04486, U04487, U04488, U04489, U04490, U04491, U04492, U04493, U04494, U04495, U04496, U04497, U04498, U04499, U04500, U04501, U04502, U04503, U04504, U04505, U04506, U04507, U04508, U04509, U04510, U04511, U04512, U04514, U04515, U04516, U04517, U04518, U04519 Genomic DNA. Translation: AAC27816.1.
U04520 expand/collapse EMBL AC list , U04470, U04471, U04472, U04473, U04474, U04476, U04477, U04478, U04479, U04480, U04483, U04485, U04486, U04487, U04488, U04489, U04490, U04491, U04492, U04493, U04494, U04495, U04496, U04497, U04498, U04499, U04500, U04501, U04502, U04503, U04504, U04505, U04506, U04507, U04508, U04509, U04510, AF199451, AF199452, U04511, U04512, U04514, U04515, U04516, U04517, U04518, U04519 Genomic DNA. Translation: AAF66217.2.
M63473 expand/collapse EMBL AC list , M63455, M63456, M63457, M63458, M63459, M63460, M63461, M63462, M63463, M63464, M63465, M63466, M63467, M63468, M63470, M63471, M63472 Genomic DNA. Translation: AAA51558.1.
M31115 mRNA. Translation: AAA52045.1.
Z37153 Genomic DNA. Translation: CAA85512.1.
S69168 mRNA. Translation: AAC60612.1.
S59334 mRNA. Translation: AAD13909.1.
S75903 Genomic DNA. Translation: AAB33374.1.
CCDSCCDS14543.1. [P29400-1]
CCDS35366.1. [P29400-2]
PIRS22917.
RefSeqNP_000486.1. NM_000495.4. [P29400-1]
NP_203699.1. NM_033380.2. [P29400-2]
XP_006724679.1. XM_006724616.1. [P29400-2]
UniGeneHs.369089.

3D structure databases

ProteinModelPortalP29400.
SMRP29400. Positions 1460-1685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107684. 9 interactions.
IntActP29400. 9 interactions.
MINTMINT-1388512.
STRING9606.ENSP00000331902.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP29400.

Polymorphism databases

DMDM461675.

Proteomic databases

MaxQBP29400.
PaxDbP29400.
PRIDEP29400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328300; ENSP00000331902; ENSG00000188153. [P29400-2]
ENST00000361603; ENSP00000354505; ENSG00000188153. [P29400-1]
GeneID1287.
KEGGhsa:1287.
UCSCuc004enz.2. human. [P29400-2]

Organism-specific databases

CTD1287.
GeneCardsGC0XP107683.
GeneReviewsCOL4A5.
H-InvDBHIX0028371.
HGNCHGNC:2207. COL4A5.
MIM301050. phenotype.
303630. gene.
neXtProtNX_P29400.
Orphanet88917. X-linked Alport syndrome.
1018. X-linked diffuse leiomyomatosis - Alport syndrome.
PharmGKBPA26722.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085652.
HOVERGENHBG004933.
KOK06237.
OMACEPGPPG.
OrthoDBEOG7RZ5P3.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP29400.
BgeeP29400.
CleanExHS_COL4A5.
GenevestigatorP29400.

Family and domain databases

Gene3D2.170.240.10. 1 hit.
InterProIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamPF01413. C4. 2 hits.
PF01391. Collagen. 22 hits.
[Graphical view]
SMARTSM00111. C4. 2 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 2 hits.
PROSITEPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL4A5. human.
GeneWikiCOL4A5.
GenomeRNAi1287.
NextBio5205.
PROP29400.
SOURCESearch...

Entry information

Entry nameCO4A5_HUMAN
AccessionPrimary (citable) accession number: P29400
Secondary accession number(s): Q16006 expand/collapse secondary AC list , Q16126, Q6LD84, Q7Z700, Q9NUB7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM