ID A0A3P9PB79_POERE Unreviewed; 1172 AA.
AC A0A3P9PB79;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Collagen alpha-1(XXVIII) chain-like {ECO:0000313|Ensembl:ENSPREP00000019166.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000019166.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000019166.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000019166.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_008419453.1; XM_008421231.1.
DR AlphaFoldDB; A0A3P9PB79; -.
DR Ensembl; ENSPRET00000019372.1; ENSPREP00000019166.1; ENSPREG00000012968.1.
DR GeneID; 103471938; -.
DR KEGG; pret:103471938; -.
DR CTD; 555428; -.
DR GeneTree; ENSGT00940000163195; -.
DR OMA; RNMPYLG; -.
DR OrthoDB; 2906665at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000012968; Expressed in head.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd01450; vWFA_subfamily_ECM; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
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; 3.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 2.
DR PRINTS; PR00759; BASICPTASE.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF53300; vWA-like; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50234; VWFA; 2.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1172
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018173662"
FT DOMAIN 55..237
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 810..993
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1119..1169
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 245..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 121213 MW; 34349F35D96E6A5C CRC64;
MNKQLTTMNV LELVKIFALI LVLSCPIKCQ NRRRKDQRDN QVITYKAKPL ACPVDIMFIV
DSTENAQPVL FEQQKTFILR FSTKLMQLHP AGWRLRLRLA ALQYSSKVSV EHNFRDWQDM
DVFQSRVASM TFIGHGSYSA YAITNATKIF RQETSPSGLR VALLMTDGRD HPRSPSAITA
AAEAKQHNIR VFTIRLSALP NPDTMGTQLR SIASAPPQQH VLSLSDSQLD EKVFSEIDTV
VTTGCPQPKN CRCEKGERGR PGSLGKPGKT GLDGAPGPKG SQGEPGTNGR PGISGLQGRS
GRKGEKGERG KFGAFGAKGG KGLAGPAGLA GRKGEEGDRG PPGDPGPEGP SGPKGDPGTR
GTPGPPGENG VGFPGLKGDK GSQGRPGSLG PMGSGEPGSQ GPMGPTGIQG SRGFPGEGLV
GPKGDRGYEG PKGSLGPPGH GHKGDKGNTG APGVPGLTGA PGSGVQGEKG EQGPIGPPGP
RGPPGLATAG SKGDQGFPGE PGHQGERGTG EPGAKGQSGT DGAPGIPGIP GEDGTVGPKG
EMGLPGPQGP EGAPGRGTSG EKGDRGDRGS RGLSGSLGPI GPAGAKGEPG SSGMVGLPGP
PGRSYPGTKG ESGPMGPSGP VGEPGVGIIG SKGNKGSVGP VGPPGPKEDS VPGPQGLPGL
TGLRGEMGPE GKGLPGATGD RGLLGVPGPS GSPGTGLPGP KGSTGQPGPP GMHGPPGEGL
PGPKGEPGFQ GPMGQRGLPG ADLSGQKGSQ GSPGHKGKKG DTGDLGPPGS PGNPGRPGEK
GESGLARDEV IQIIKEIFGC GVMCREIPLE LVFVIDISES VGPENFEVVK DFVNAIIDQF
TVSQEASRVG VVLYSHLNTV VVGLQQQPSR EEIKAAVRAM PFLGEGTFTG SAMLQARKVF
RDSRPHVRRV AVVLTDVQSD QRDLVQFKET ASETHAEGIE VLIIGVVKKT DPLYEEFLSE
MKTVASDPKE EHVYIIDDFL LLPVLENYIL KQICDRDAAA PFSPKSFSSA ETHPNGPEDT
ESKKIPEAKN TRPPAPQPTE SLWSHEDQFD PEVTVEPSNK QPSLPFTPHG EKGESGPGQN
SVVQRQSPTD WPGEVESFHT TFGPPPPTLT VSPASGEGCS QPLEPGPCRQ YRIRWYYDPE
ANACAQFWYG GCQGNANNFE NEANCRNTCI YT
//
