ID   CO4A5_CANLF             Reviewed;        1691 AA.
AC   Q28247; Q866Z2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Collagen alpha-5(IV) chain;
DE   Flags: Precursor;
GN   Name=COL4A5;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RX   PubMed=12879362; DOI=10.1007/s00335-002-2253-9;
RA   Cox M.L., Lees G.E., Kashtan C.E., Murphy K.E.;
RT   "Genetic cause of X-linked Alport syndrome in a family of domestic dogs.";
RL   Mamm. Genome 14:396-403(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 925-1684, AND DISEASE.
RC   STRAIN=Samoyed; TISSUE=Kidney;
RX   PubMed=8171024; DOI=10.1073/pnas.91.9.3989;
RA   Zheng K., Thorner P.S., Marrano P., Baumal R., McInnes R.R.;
RT   "Canine X chromosome-linked hereditary nephritis: a genetic model for human
RT   X-linked hereditary nephritis resulting from a single base mutation in the
RT   gene encoding the alpha 5 chain of collagen type IV.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3989-3993(1994).
CC   -!- FUNCTION: Type IV collagen is the major structural component of
CC       glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork
CC       together with laminins, proteoglycans and entactin/nidogen.
CC   -!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha
CC       6(IV), each of which can form a triple helix structure with 2 other
CC       chains to generate type IV collagen network.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain
CC       (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats
CC       in the long central triple-helical domain (which may cause flexibility
CC       in the triple helix), and a short N-terminal triple-helical 7S domain.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC       (G-X-Y) are hydroxylated in some or all of the chains.
CC   -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC       involved in inter- and intramolecular disulfide bonding. 12 of these,
CC       located in the NC1 domain, are conserved in all known type IV
CC       collagens.
CC   -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC       covalent bonds between Lys and Met residues. {ECO:0000250}.
CC   -!- DISEASE: Note=A defect in COL4A5 has been found to be the cause of
CC       canine X-linked hereditary nephritis (HN), a disease similar to that in
CC       humans (also referred to as Alport syndrome) characterized by
CC       progressive renal failure and neurosensory deafness.
CC       {ECO:0000269|PubMed:12879362, ECO:0000269|PubMed:8171024}.
CC   -!- SIMILARITY: Belongs to the type IV collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00736}.
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DR   EMBL; AF470624; AAO33458.2; -; mRNA.
DR   EMBL; U07888; AAB60258.1; -; mRNA.
DR   PIR; A55267; A55267.
DR   RefSeq; NP_001002979.1; NM_001002979.1.
DR   AlphaFoldDB; Q28247; -.
DR   STRING; 9612.ENSCAFP00000026629; -.
DR   PaxDb; Q28247; -.
DR   PRIDE; Q28247; -.
DR   GeneID; 403466; -.
DR   KEGG; cfa:403466; -.
DR   CTD; 1287; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   InParanoid; Q28247; -.
DR   OrthoDB; 63831at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   Gene3D; 2.170.240.10; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR001442; Collagen_IV_NC.
DR   InterPro; IPR036954; Collagen_IV_NC_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF01413; C4; 2.
DR   Pfam; PF01391; Collagen; 19.
DR   SMART; SM00111; C4; 2.
DR   SUPFAM; SSF56436; SSF56436; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
PE   2: Evidence at transcript level;
KW   Alport syndrome; Basement membrane; Cell adhesion; Collagen;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1691
FT                   /note="Collagen alpha-5(IV) chain"
FT                   /id="PRO_0000005851"
FT   DOMAIN          1467..1691
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   REGION          27..41
FT                   /note="Nonhelical region (NC2)"
FT   REGION          42..1462
FT                   /note="Triple-helical region"
FT   REGION          49..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..213
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..279
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..402
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..725
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..766
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..833
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..880
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1054
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1166
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1267
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1414
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        451
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        481
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        484
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1482..1573
FT                   /note="Or C-1482 with C-1570"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1515..1570
FT                   /note="Or C-1515 with C-1573"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1527..1533
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1592..1687
FT                   /note="Or C-1592 with C-1684"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1626..1684
FT                   /note="Or C-1626 with C-1687"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1638..1644
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   CROSSLNK        1555
FT                   /note="S-Lysyl-methionine sulfilimine (Met-Lys) (interchain
FT                   with K-1673)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        1673
FT                   /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain
FT                   with M-1555)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        925
FT                   /note="N -> D (in Ref. 2; AAB60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1158
FT                   /note="G -> W (in Ref. 2; AAB60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1265..1270
FT                   /note="Missing (in Ref. 2; AAB60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1575
FT                   /note="A -> R (in Ref. 2; AAB60258)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1691 AA;  162237 MW;  513DB6DAB4C3C68D CRC64;
     MKLRGVSLAA GWFLLALSLW GQPAEAAACY GCSPGSKCDC SGVKGEKGER GFPGLEGHPG
     LPGFPGPEGP PGPRGQKGDD GIRGPPGPKG IRGPPGLPGF PGTPGLPGMP GHDGAPGPQG
     IPGCNGTKGE RGFPGSPGFP GLEGPPGPPG IPGMKGEPGS IIMSSLPGPK GNPGYPGPPG
     IQGPAGPTGL PGPIGPPGPP GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP
     PGQISEQKRP IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGMKGEKGE QGEPGKRGKP
     GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDIGSTG PPGLVIPRPG TGVTVGEKGN
     MGLPGLPGEK GERGFPGIQG PPGLPGPPGT AVMGPPGPPG FPGERGQKGD EGPPGISIPG
     FPGLDGQPGA PGLRGPPGPP GPHISPSDEI CETGPPGPPG SPGDRGLQGE QGVKGDKGDT
     CFNCIGTGVS GPRGQPGLPG LPGPPGSLGF PGQKGEKGHA GLTGPKGLTG IPGAPGPPGF
     PGSKGEPGDV LTFPGMKGDK GELGYPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGIAFKG
     ERGPPGNPGL PGLPGNRGPM GPVGFGPPGP VGEKGIQGVA GNPGQPGIPG PKGDPGQTIT
     QPGKPGLPGN PGRHGEVGLP GDPGLPGPPG LPGIPGNKGE PGIPGIGLPG PPGPKGFPGI
     QGPPGAPGTP GRIGLEGPSG PPGFPGPKGE PGLGLPGPPG PPGLPGFKGT LGPKGDRGFP
     GPPGLPGRTG LDGLPGPKGD VGPKGQPGPM GPPGLPGIGV QGPPGPPGIP GPVGEPGLHG
     IPGEKGDPGP PGFDVLGPPG ERGSPGIPGA PGPMGPPGTP GLPGKAGASG FPGAKGEMGM
     MGPPGPPGPL GIPGRSGVPG LKGDNGLQGQ PGPPGPEGEK GGKGEPGLPG PPGPVDPDLL
     GSKGEKGDPG LPGIPGVSGP KGYQGLPGDP GQPGLSGQPG LPGPSGPKGN PGLPGKPGLT
     GPPGLKGSIG DMGFPGPQGV KGSPGPPGVP GQPGSPGLPG QKGEKGDPGV SGIGLPGLPG
     PKGEAGLPGY PGNPGIKGSM GDTGLPGLPG TPGAKGQPGL PGFPGTPGLP GPKGINGPPG
     NPGLPGEPGP VGGGGRPGPP GPPGEKGNPG QDGIPGPAGQ KGEPGQPGFG IPGPPGLPGL
     SGQKGDGGLP GIPGNPGLPG PKGEPGFQGF PGVQGPPGPP GSPGPALEGP KGNPGPQGPP
     GRPGPTGFQG LPGPEGPRGL PGNGGIKGER GNPGQPGQPG LPGLKGDQGP PGIQGNPGRP
     GLNGMKGDPG LPGVPGFPGM KGPSGVPGSA GPEGDPGLVG PPGPPGLPGP SGQSIIIKGD
     VGPPGIPGQP GLKGLPGLPG PQGLPGPIGP PGDPGRNGLP GFDGAGGRKG DPGLPGQPGT
     RGLDGPPGPD GMQGPPGPPG TSSIAHGFLI TRHSQTTDAP QCPHGTVQIY EGFSLLYVQG
     NKRAHGQDLG TAGSCLRRFS TMPFMFCNIN NVCNFASRND YSYWLSTPEP MPMSMEPLKG
     QSIQPFISRC AVCEAPAVVI AVHSQTIQIP HCPHGWDSLW IGYSFMMHTS AGAEGSGQAL
     ASPGSCLEEF RSAPFIECHG RGTCNYYANS YSFWLATVDV SDMFSKPQSE TLKAGDLRTR
     ISRCQVCMKR T