P29400 (CO4A5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-5(IV) chain

Gene names

Name:

COL4A5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1685 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular matrix › basement 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.

Ontologies

Keywords
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Alport syndrome Deafness Disease mutation
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome collagen catabolic process Traceable author statement. Source: Reactome extracellular matrix disassembly Traceable author statement. Source: Reactome neuromuscular junction development Inferred from electronic annotation. Source: Compara
Cellular_component	basal lamina Inferred from electronic annotation. Source: Compara collagen type IV Traceable author statement PubMed 2349482. Source: ProtInc endoplasmic reticulum lumen Traceable author statement. Source: Reactome neuromuscular junction Inferred from electronic annotation. Source: Compara
Molecular_function	extracellular matrix structural constituent Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 1685	1659	Collagen alpha-5(IV) chain		PRO_0000005852
Regions
	Domain	1461 – 1685	225	Collagen IV NC1
	Region	27 – 41	15	Nonhelical region (NC2)
	Region	42 – 1456	1415	Triple-helical region
Amino acid modifications
	Glycosylation	125	1	N-linked (GlcNAc...) Potential
	Disulfide bond	451		Interchain Potential
	Disulfide bond	481		Interchain Potential
	Disulfide bond	484		Interchain Potential
	Disulfide bond	1476 ↔ 1567		Or C-1476 with C-1564 By similarity
	Disulfide bond	1509 ↔ 1564		Or C-1509 with C-1567 By similarity
	Disulfide bond	1521 ↔ 1527		By similarity
	Disulfide bond	1586 ↔ 1681		Or C-1586 with C-1678 By similarity
	Disulfide bond	1620 ↔ 1678		Or C-1620 with C-1681 By similarity
	Disulfide bond	1632 ↔ 1638		By similarity
	Cross-link	1549		S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1667) By similarity
	Cross-link	1667		S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1549) By similarity
Natural variations
	Alternative sequence	1264	1	G → GPTGFQG in isoform 2.		VSP_001173
	Natural variant	54	1	G → D in APSX; adult type.		VAR_001914
	Natural variant	114	1	G → S in APSX.		VAR_007991
	Natural variant	129	1	G → E in APSX; juvenile type.		VAR_001915
	Natural variant	129	1	G → V in APSX; juvenile type.		VAR_001916
	Natural variant	174	1	G → R in APSX. Ref.24		VAR_001917
	Natural variant	177	1	G → C in APSX; presenting with dot-and-fleck retinopathy. Ref.29		VAR_011220
	Natural variant	177	1	G → R in APSX; adult type. Ref.24		VAR_001918
	Natural variant	192	1	G → R in APSX. Ref.32		VAR_011221
	Natural variant	204	1	G → V in APSX; juvenile type.		VAR_011222
	Natural variant	216	1	G → R in APSX; juvenile type. Ref.30		VAR_001919
	Natural variant	219	1	G → S in APSX.		VAR_001920
	Natural variant	230	1	G → R in APSX; juvenile type.		VAR_011223
	Natural variant	239	1	G → E in APSX.		VAR_011224
	Natural variant	264	1	G → R in APSX; adult type.		VAR_011225
	Natural variant	289	1	G → V in APSX; juvenile type.		VAR_001921
	Natural variant	292	1	G → R in APSX. Ref.32		VAR_011226
	Natural variant	292	1	G → V in APSX; juvenile type.		VAR_001922
	Natural variant	295	1	G → D in APSX. Ref.32		VAR_011227
	Natural variant	298	1	G → S in APSX.		VAR_011228
	Natural variant	319	1	G → R in APSX; juvenile type. Ref.31		VAR_011229
	Natural variant	325	1	G → E in APSX. Ref.15		VAR_001923
	Natural variant	325	1	G → R in APSX; juvenile and adult types. Ref.14 Ref.24 Ref.32		VAR_001924
	Natural variant	331	1	G → V in APSX.		VAR_007992
	Natural variant	365 – 367	3	Missing in APSX; juvenile type.		VAR_001926
	Natural variant	365	1	G → E in APSX; juvenile type.		VAR_001925
	Natural variant	371	1	G → E in APSX; juvenile type.		VAR_001927
	Natural variant	374	1	G → A in APSX.		VAR_001928
	Natural variant	383	1	G → D in APSX; juvenile type.		VAR_001929
	Natural variant	400	1	G → E in APSX; adult type. Ref.18		VAR_001930
	Natural variant	406	1	G → V in APSX; adult type. Ref.18		VAR_001931
	Natural variant	409	1	G → D in APSX.		VAR_001932
	Natural variant	412	1	G → V in APSX; adult type.		VAR_011230
	Natural variant	415	1	G → R in APSX. Ref.30		VAR_011231
	Natural variant	420	1	G → E in APSX; juvenile type.		VAR_011232
	Natural variant	420	1	G → V in APSX. Ref.25		VAR_011233
	Natural variant	423	1	G → E in APSX.		VAR_011234
	Natural variant	430	1	A → D. Ref.21		VAR_001933
	Natural variant	444	1	I → S. Ref.21 Ref.26 Ref.32 Corresponds to variant rs2272946 [ dbSNP | Ensembl ].		VAR_001934
	Natural variant	456 – 458	3	Missing in APSX.		VAR_001935
	Natural variant	466	1	G → E in APSX.		VAR_001936
	Natural variant	472	1	G → R in APSX.		VAR_007993
	Natural variant	491	1	G → E in APSX; juvenile type.		VAR_011235
	Natural variant	494	1	G → D in APSX; adult type.		VAR_001937
	Natural variant	496 – 507	12	Missing in APSX; juvenile type.		VAR_001938
	Natural variant	497	1	G → C in APSX; adult type.		VAR_011236
	Natural variant	521	1	G → C in APSX. Ref.4		VAR_001939
	Natural variant	521	1	G → S in APSX.		VAR_001940
	Natural variant	524	1	G → D in APSX; adult type.		VAR_011237
	Natural variant	545	1	G → R in APSX.		VAR_007994
	Natural variant	545	1	G → V in APSX.		VAR_007995
	Natural variant	558	1	G → R in APSX. Ref.32		VAR_011238
	Natural variant	561	1	G → R in APSX.		VAR_007996
	Natural variant	567	1	G → A in APSX; juvenile type.		VAR_001941
	Natural variant	573	1	G → D in APSX. Ref.25		VAR_011239
	Natural variant	579	1	G → E in APSX. Ref.26		VAR_011240
	Natural variant	579	1	G → R in APSX; adult type.		VAR_007997
	Natural variant	603	1	G → V in APSX. Ref.32		VAR_011241
	Natural variant	609	1	G → R in APSX; juvenile type.		VAR_011242
	Natural variant	609	1	G → V in APSX; juvenile type.		VAR_001942
	Natural variant	619	1	P → S. Ref.21		VAR_011243
	Natural variant	621	1	G → C in APSX.		VAR_011244
	Natural variant	624	1	G → D in APSX. Ref.25 Ref.32		VAR_011245
	Natural variant	629	1	G → D in APSX. Ref.32		VAR_011246
	Natural variant	632	1	G → D in APSX.		VAR_011247
	Natural variant	633	1	E → K in APSX. Ref.26		VAR_011248
	Natural variant	635	1	G → D in APSX. Ref.25		VAR_007998
	Natural variant	638	1	G → A in APSX. Ref.18		VAR_001944
	Natural variant	638	1	G → S in APSX; juvenile type.		VAR_007999
	Natural variant	638	1	G → V in APSX. Ref.18		VAR_001943
	Natural variant	653	1	G → R in APSX; juvenile type. Ref.18		VAR_001945
	Natural variant	664	1	K → N. Ref.21 Corresponds to variant rs34077552 [ dbSNP | Ensembl ].		VAR_001946
	Natural variant	669	1	G → A in APSX; juvenile type.		VAR_008000
	Natural variant	681	1	G → D in APSX.		VAR_011249
	Natural variant	684	1	G → V in APSX; adult type.		VAR_001947
	Natural variant	687	1	G → E in APSX.		VAR_008001
	Natural variant	722	1	G → E in APSX. Ref.32		VAR_011250
	Natural variant	739	1	P → A. Ref.26		VAR_011251
	Natural variant	739	1	P → S in APSX; juvenile type. Ref.31		VAR_011252
	Natural variant	740	1	G → E in APSX; juvenile type.		VAR_001948
	Natural variant	743	1	G → D in APSX.		VAR_008002
	Natural variant	772	1	G → D in APSX; juvenile type.		VAR_001949
	Natural variant	796	1	G → R in APSX. Ref.18		VAR_001950
	Natural variant	802 – 807	6	Missing in APSX.		VAR_011254
	Natural variant	802	1	G → R in APSX.		VAR_011253
	Natural variant	808	1	G → E in APSX; adult type.		VAR_008003
	Natural variant	811	1	G → V in APSX; juvenile type.		VAR_011255
	Natural variant	822 – 824	3	Missing in APSX.		VAR_008004
	Natural variant	822	1	G → R in APSX. Ref.27		VAR_011256
	Natural variant	852	1	G → E in APSX; juvenile type.		VAR_008005
	Natural variant	852	1	G → R in APSX.		VAR_001951
	Natural variant	864 – 875	12	Missing in APSX.		VAR_011257
	Natural variant	866	1	G → E in APSX; adult type.		VAR_001952
	Natural variant	869	1	G → R in APSX; juvenile type. Ref.18 Ref.25		VAR_001953
	Natural variant	872	1	G → R in APSX. Ref.18		VAR_001954
	Natural variant	878	1	G → R in APSX.		VAR_008006
	Natural variant	898	1	M → V in APSX; mild phenotype. Ref.32		VAR_011258
	Natural variant	902	1	G → V in APSX; juvenile type. Ref.31		VAR_011259
	Natural variant	911	1	G → E in APSX. Ref.31		VAR_011260
	Natural variant	941	1	G → C in APSX. Ref.25		VAR_011261
	Natural variant	942	1	Missing in APSX.		VAR_001955
	Natural variant	947	1	G → D in APSX. Ref.26		VAR_011262
	Natural variant	953	1	G → V in APSX; found on the same allele as variant Glu-1211. Ref.26		VAR_011263
	Natural variant	988 – 992	5	Missing in APSX; adult type.		VAR_008007
	Natural variant	1006	1	G → A in APSX. Ref.32		VAR_011264
	Natural variant	1006	1	G → V in APSX. Ref.32		VAR_011265
	Natural variant	1015	1	G → E in APSX.		VAR_011266
	Natural variant	1015	1	G → V in APSX.		VAR_011267
	Natural variant	1030	1	G → S in APSX. Ref.25		VAR_011268
	Natural variant	1036	1	G → V in APSX.		VAR_011269
	Natural variant	1039	1	G → S in APSX; juvenile type.		VAR_011270
	Natural variant	1045	1	G → E in APSX. Ref.30		VAR_011271
	Natural variant	1066	1	G → R in APSX.		VAR_011272
	Natural variant	1066	1	G → S in APSX. Ref.25		VAR_011273
	Natural variant	1086	1	G → D in APSX. Ref.30		VAR_011274
	Natural variant	1104	1	G → V in APSX.		VAR_001956
	Natural variant	1107	1	G → R in APSX. Ref.26		VAR_008008
	Natural variant	1143	1	G → D in APSX; juvenile type. Ref.25		VAR_001957
	Natural variant	1143	1	G → S in APSX; adult type.		VAR_001958
	Natural variant	1158	1	G → R in APSX. Ref.26		VAR_011275
	Natural variant	1161	1	G → R in APSX.		VAR_008009
	Natural variant	1167	1	G → S in APSX. Ref.30		VAR_011276
	Natural variant	1170	1	G → S in APSX. Ref.26		VAR_011277
	Natural variant	1182	1	G → R in APSX; juvenile type.		VAR_001959
	Natural variant	1196	1	G → R in APSX. Ref.25		VAR_011278
	Natural variant	1205	1	G → C in APSX; juvenile type.		VAR_011279
	Natural variant	1211	1	G → E in APSX; found on the same allele as variant Val-953.		VAR_011280
	Natural variant	1211	1	G → R in APSX.		VAR_008010
	Natural variant	1220	1	G → D in APSX.		VAR_008011
	Natural variant	1229	1	G → D in APSX; adult type. Ref.31		VAR_011281
	Natural variant	1241	1	G → C in APSX. Ref.18		VAR_001960
	Natural variant	1244	1	G → D in APSX. Ref.32		VAR_011282
	Natural variant	1252	1	G → S in APSX; adult type.		VAR_011283
	Natural variant	1261	1	G → E in APSX. Ref.25		VAR_011284
	Natural variant	1270	1	G → S in APSX.		VAR_001961
	Natural variant	1333	1	G → S in APSX.		VAR_008012
	Natural variant	1357	1	G → S in APSX. Ref.25		VAR_011285
	Natural variant	1379	1	G → V in APSX; adult type.		VAR_001962
	Natural variant	1410	1	R → C in APSX; adult and juvenile types. Ref.24		VAR_001963
	Natural variant	1421	1	G → W in APSX; adult type. Ref.24		VAR_001964
	Natural variant	1422	1	R → C in APSX; juvenile type.		VAR_001965
	Natural variant	1427	1	G → V in APSX; adult type.		VAR_008013
	Natural variant	1428	1	L → M. Ref.21		VAR_011286
	Natural variant	1442	1	G → D in APSX.		VAR_008014
	Natural variant	1451	1	G → S in APSX.		VAR_001966
	Natural variant	1486	1	G → A in APSX; adult type.		VAR_008015
	Natural variant	1488	1	S → F in APSX.		VAR_011287
	Natural variant	1498	1	A → D in APSX. Ref.22		VAR_001967
	Natural variant	1511	1	R → H in APSX; juvenile type; could be a non pathogenic variant. Ref.31		VAR_011288
	Natural variant	1517	1	P → T in APSX; juvenile type. Ref.16 Ref.24		VAR_001968
	Natural variant	1538	1	W → S in APSX; adult type. Ref.16		VAR_001969
	Natural variant	1559	1	P → A.		VAR_008016
	Natural variant	1563	1	R → Q in APSX. Ref.16		VAR_001970
	Natural variant	1564	1	C → S in APSX; adult type. Ref.13		VAR_001971
	Natural variant	1567	1	C → R in APSX; juvenile type.		VAR_011289
	Natural variant	1596	1	G → D in APSX. Ref.24		VAR_001972
	Natural variant	1597 – 1685	89	Missing in APSX.		VAR_019594
	Natural variant	1649	1	L → R in APSX; adult type. Ref.19 Ref.25 Ref.32		VAR_001973
	Natural variant	1677	1	R → P in APSX. Ref.32		VAR_011290
	Natural variant	1677	1	R → Q in APSX. Ref.23		VAR_001974
	Natural variant	1678	1	C → W in APSX. Ref.26		VAR_011291
	Natural variant	1679 – 1685	7	Missing in APSX.		VAR_019595
Experimental info
	Sequence conflict	440 – 441	2	AG → GS in AAA99480. Ref.5
	Sequence conflict	625 – 628	4	FGPP → LALQ in AAA99480. Ref.5
	Sequence conflict	667 – 668	2	LP → FR in AAA99480. Ref.5
	Sequence conflict	888	1	A → R in AAA99480. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 4450A6762F12A626	FASTA	1,685	161,044
	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
	Isoform 2 [UniParc]. Checksum: E45612A1C153D123	FASTA	1,691	161,632
	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 GRPGPTGFQG LPGPEGPPGL PGNGGIKGEK GNPGQPGLPG LPGLKGDQGP PGLQGNPGRP 1330 1340 1350 1360 1370 1380 GLNGMKGDPG LPGVPGFPGM KGPSGVPGSA GPEGEPGLIG PPGPPGLPGP SGQSIIIKGD 1390 1400 1410 1420 1430 1440 AGPPGIPGQP GLKGLPGPQG PQGLPGPTGP PGDPGRNGLP GFDGAGGRKG DPGLPGQPGT 1450 1460 1470 1480 1490 1500 RGLDGPPGPD GLQGPPGPPG TSSVAHGFLI TRHSQTTDAP QCPQGTLQVY EGFSLLYVQG 1510 1520 1530 1540 1550 1560 NKRAHGQDLG TAGSCLRRFS TMPFMFCNIN NVCNFASRND YSYWLSTPEP MPMSMQPLKG 1570 1580 1590 1600 1610 1620 QSIQPFISRC AVCEAPAVVI AVHSQTIQIP HCPQGWDSLW IGYSFMMHTS AGAEGSGQAL 1630 1640 1650 1660 1670 1680 ASPGSCLEEF RSAPFIECHG RGTCNYYANS YSFWLATVDV SDMFSKPQSE TLKAGDLRTR 1690 ISRCQVCMKR T

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

Web resources

GeneReviews

Alport syndrome and COL4A5

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 , 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 , 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 , 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.
IPI	IPI00021715. IPI00216007.
PIR	S22917.
RefSeq	NP_000486.1. NM_000495.4. NP_203699.1. NM_033380.2.
UniGene	Hs.369089.
3D structure databases
ProteinModelPortal	P29400.
ModBase	Search...
Protein-protein interaction databases
IntAct	P29400. 2 interactions.
MINT	MINT-1388512.
STRING	9606.ENSP00000331902.
PTM databases
PhosphoSite	P29400.
Polymorphism databases
DMDM	461675.
Proteomic databases
PaxDb	P29400.
PRIDE	P29400.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000328300; ENSP00000331902; ENSG00000188153. ENST00000361603; ENSP00000354505; ENSG00000188153.
GeneID	1287.
KEGG	hsa:1287.
UCSC	uc004enz.1. human.
Organism-specific databases
CTD	1287.
GeneCards	GC0XP107683.
H-InvDB	HIX0028371.
HGNC	HGNC:2207. COL4A5.
MIM	301050. phenotype. 303630. gene.
neXtProt	NX_P29400.
Orphanet	88917. X-linked Alport syndrome. 1018. X-linked diffuse leiomyomatosis - Alport syndrome.
PharmGKB	PA26722.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000085652.
HOVERGEN	HBG004933.
KO	K06237.
OMA	CEPGPPG.
PhylomeDB	P29400.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P29400.
Bgee	P29400.
CleanEx	HS_COL4A5.
Genevestigator	P29400.
GermOnline	ENSG00000188153. Homo sapiens.
Family and domain databases
Gene3D	2.170.240.10. 1 hit.
InterPro	IPR016187. C-type_lectin_fold. IPR008160. Collagen. IPR001442. Collagen_VI_NC. [Graphical view]
Pfam	PF01413. C4. 2 hits. PF01391. Collagen. 22 hits. [Graphical view]
SMART	SM00111. C4. 2 hits. [Graphical view]
SUPFAM	SSF56436. C-type_lectin_fold. 2 hits.
PROSITE	PS51403. NC1_IV. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	COL4A5. human.
GenomeRNAi	1287.
NextBio	5205.
SOURCE	Search...

Entry information

Entry name

CO4A5_HUMAN

Accession

Primary (citable) accession number: P29400
Secondary accession number(s): Q16006 , Q16126, Q6LD84, Q7Z700, Q9NUB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	February 1, 1994
Last modified:	May 29, 2013
This is version 158 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.