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Database: UniProt
Entry: A0A3P9QEM8_POERE
LinkDB: A0A3P9QEM8_POERE
Original site: A0A3P9QEM8_POERE 
ID   A0A3P9QEM8_POERE        Unreviewed;      1195 AA.
AC   A0A3P9QEM8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   28-JAN-2026, entry version 31.
DE   SubName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0000313|Ensembl:ENSPREP00000032611.1};
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:ENSPREP00000032611.1, 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:ENSPREP00000032611.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000032611.1};
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSPREP00000032611.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000032611.1};
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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DR   AlphaFoldDB; A0A3P9QEM8; -.
DR   Ensembl; ENSPRET00000032980.1; ENSPREP00000032611.1; ENSPREG00000022058.1.
DR   GeneTree; ENSGT00940000164061; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000022058; Expressed in caudal fin and 1 other cell type or tissue.
DR   GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1195
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017942691"
FT   DOMAIN          34..223
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          222..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..252
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..299
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..348
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..394
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..423
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..456
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..471
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..545
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..584
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..639
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..655
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..745
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..769
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..791
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..891
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  121662 MW;  F29729178C6B1CE3 CRC64;
     MASRIPPWFF GLSLLCCHHS SAYQLLDDRG SHSSLDLTEL IGVPLPPSVS FVTGFEGYPA
     YSFGPGANVG RLTKSFIPDP FHHDFAITVM AKPTTRRGGV LFAITDAYQK VVQLGVALSE
     VEDGAQNVIL YYTDPETRGG TREAASFKMG EVTGRWARFT LTVQGAEIRL YMDCEEYHRV
     AFTRSAQPLT FQTSSGIFVG NAGGTGLPRF VGSIQKLLLN SDPTAPDDQC EEDDPYASGF
     GSGDEDYDDS KEGDEVKKIV EEREYPMVFP DPTYGGPVQA PPTEPSLIDD EEGDDEESSG
     QEMEMTTVRA ATSRANASER RADASLQVST GQKGEPGEPG PPGSPGPPGQ AVGGGGDPGP
     RGPAGPTGLP GKDGEPGMKG ERGLPGAAGF PGLPGDSGPK GEKGDPGLGV PGPPGPPGAP
     GPPSKAVMEG SGFEDFDSDT EVVRGPPGPP GPPGLPGLPG SSASGVAPGP AGKDGANGEP
     GLAGVDGKDG DPGPAGEKGA KGEPGASGPP GPKGDQGPAG FPGLPGSPGA EGQPGPRGPP
     GPPGPSGSRF ATTLEDLEGS GLLEDFGGSP GPQGPPGVPG PPGPKGADGS DGNPGKPGQK
     GEQGVSGPPG LPGLDGMKGE KGANGNKGDP GIKGERGRDG VGVPGPPGRP GPPGPVINLQ
     DLLLNATDGA FNFSGVFQTQ VPAGPKGDVG LQGLQGPPGI KGEKGEPGFL TGPDGSLMSD
     LAGALGTKGI KGDDGVPGAP GVSGPVGPPG PKGEIGFPGR QGRPGLLGPK GEKGDLHGLP
     GPPGPPGPPG KPGMFNCPKG LHPNGTVASG NCHQGAKGEK GERGLPGLPA PQSSFLPTGG
     WLTKGDQGMK GEKGEAGFPG QPGIPGRSGL VGPKGESVLG PPGPPGMPGP PGAAGYGRPG
     AVGPPGPPGP PGLPLRYGSA VAIAGPPGPP GPPGAPGTSS NSAFLKTFST RESMMQQTSR
     DEEGTLAYVK ATGNLFLKVP QGWKQIQLGS LIYLSNNIIP QDEPRVAYQV RGETMQRVRS
     VKERLNLVAL NQPHSGNMMG LDMADRMCYE QAKAMGLAPN YRAFISSHKQ DLVHVVYPGF
     RDSLPVTNLR GDVMFRNWQS IFIGNGGPVN PRIPIYSFDG RDVLADPFWP KKSIWHGSTS
     RGLRVIDKHC ETWQADDFSV MGQSSSLTSG LLLGQQTRSC STEFIVLCIE TYKNS
//
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