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Database: UniProt
Entry: A0A060YA50_ONCMY
LinkDB: A0A060YA50_ONCMY
Original site: A0A060YA50_ONCMY 
ID   A0A060YA50_ONCMY        Unreviewed;       871 AA.
AC   A0A060YA50;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Collagen alpha-1(XXVIII) chain {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GSONMT00008804001 {ECO:0000313|EMBL:CDQ88798.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ88798.1, ECO:0000313|Proteomes:UP000193380};
RN   [1] {ECO:0000313|EMBL:CDQ88798.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24755649; DOI=10.1038/ncomms4657;
RA   Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA   Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA   Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA   Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA   Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA   Guiguen Y.;
RT   "The rainbow trout genome provides novel insights into evolution after
RT   whole-genome duplication in vertebrates.";
RL   Nat. Commun. 5:3657-3657(2014).
RN   [2] {ECO:0000313|EMBL:CDQ88798.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FR908961; CDQ88798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060YA50; -.
DR   STRING; 8022.A0A060YA50; -.
DR   PaxDb; 8022-A0A060YA50; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN ALPHA-1(X) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..871
FT                   /note="Collagen alpha-1(XXVIII) chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001591807"
FT   DOMAIN          473..653
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          810..860
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          73..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  89797 MW;  2222B0B5FCF4EBB6 CRC64;
     MLLSLFAATF NLCLLCLSSQ GDRGQAGPAG IQGENGIGLP GPKVHLVCFC FCLTNELFYV
     TCSISPWPQG FQGEKGPHGE GLPGPKGDRG LAGPRGPRGQ TGAGIKGEKG EFGPPGHPGL
     VGLTGAGIQG EKGVEGPRGP PGGRGPQGEG LPGPKGDQGF PGELGATGER GVGEPGPKGE
     LGTSGLAGLP GLPGEDGAPG QKGEAGVAGI RGPDGAAGIG TQGEKGDQGQ RGIRGLHGPP
     GMTGPSGAKG EPGTPGRLGM PGLPGRAIAG PKGDLGPPGP SGPTGETGYG LPGPKGDRGN
     PGPTGPFGSK GEGCARTTGM KLILTELPLF SHRSHSECNT LTHTGSPAVM AMSKLNQLYI
     IGFQGNIGRK GPPGPNGPPG EGLQGPKGEQ GSQGVTGPRG PIGEGFPGGK GDRGLQGERG
     NKGVKGGMGD SGVPGESGRP GVKGEVGLTR EDIIKLIKEI CGCGIKCKER PMELVFVIDS
     SESVGPENFE IIKDFVTALV DRTTVGRNAT RIGLVLYSLD VHLEFNLARY MTKQDVKQAI
     RKMSYVGEGT YTSTAIRKAT QEAFYSARTG VRKVAIVITD GQTDKREPVK LDIAVREAHA
     ANIEMYALGI VNTSDTTQAE FLRELNLIAS DPDSEHMYLI DDFNTLPALE SKLVSQFCED
     ENGALGNSGH GNSGQGNSGH GNNGHLNNEH GNTYNEDPIL NPSGRTSSQS HIRGRGDNFD
     LPLNAGPLPV QVQVDDEEGE DLDVRTHVRG GSTVAVANKT VSIFPAKESS HSNTAVSSSG
     SASSSSGTTG SASSSSEGQF QPSVSLNPRC NLSLDQGTCR EYNIQWYYDK QANSCAQFWY
     GSCEGNANRF ETEDACKKTC VLSRTGMCRS S
//
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