ID A0A3P9Q8K3_POERE Unreviewed; 1370 AA.
AC A0A3P9Q8K3;
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 type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSPREP00000030329.1};
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:ENSPREP00000030329.1, 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:ENSPREP00000030329.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000030329.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPREP00000030329.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000030329.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR RefSeq; XP_008402482.1; XM_008404260.2.
DR STRING; 8081.ENSPREP00000030329; -.
DR Ensembl; ENSPRET00000030673.1; ENSPREP00000030329.1; ENSPREG00000020512.1.
DR GeneID; 103461887; -.
DR KEGG; pret:103461887; -.
DR CTD; 564123; -.
DR GeneTree; ENSGT00940000165423; -.
DR OMA; VQDQHQN; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
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; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1370
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018154793"
FT DOMAIN 118..307
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 167..306
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 83..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..406
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..654
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..739
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..775
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..898
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1006
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1048
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1075
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 139651 MW; 84BBC44FA2429161 CRC64;
MRSWFKALPL LTLWVVYSEA WFWSWSETGT TLAPRLELEG SGIATGSGEP PSESSTTAGA
EIIDEGHVLQ TVGQTWDETT EGPRVTTVVP STQPERGRGA GKTTAGITSR RSKPEDSGVT
LLQLIGDPPP EKIPEVDGPD NSPAYLFGPE SATGQLARAH FPNPFYRNFA LIFSLKPTSD
DGGIVFSITD SSQQVMHLGV KLSAVQGSEQ NVVLFYSEAG AGQSKEAARF RVPSMTNAWN
RFAVAVKDDK AMLYLNCDVE PQVMRMERLA GELELESGSG VFVGQAGGEH PDKFKGAISE
LRVVGDPSAA ARFCEEDDDS DMASGEGSGY EETRRPKPLS EKPQQTTADE SLPPIQQPPL
EQPVQKAQTG AVAAKGEKGD RGEKGDRGPA GPKGDAGSGS QGGIRGLKGE PGEKGAKGSA
GFGYPGSKGE PGPPGPPGPP GSPGAATQYS VDRDGSVVSK VPGPRGPPGP AGPQGPPGED
GEPGDPGEDG KTGPQGPPGF PGTLGDAGAK GEKGDRGEGQ PGPRGPPGPP GPPGTGYRST
FEDMEASGFP DLVSVRGLPG PPGLPGPPGP PGLPSASTSV NSGAFGPPGK NGAPGQPGLP
GLPGADGLPG APGPRGEKGD SGDLGLPGAI GQKGSLGESG LPGPAGEPGL AGLPGPMGPV
GPPGPPGPPG QGHRVGFDDM EDSSGIFTNG LPGVRGPEGI QGPPGLPGHP GKPGFPGIQG
PKGEQGLAGR DGLPGLDGFP GPPGQKGDRG DKGETGDAGR DGNGLPGPPG PPGPPGQIIY
QPSDNGVAGL PGRAGFPGPV GPKGDRGDPG SPGYGPKGEK GEPGLIIGPD GNPLYLGGLT
GTKGDRGLPG PIGPFGPQGP PGLKGEIGMP GRPGRPGVNG YKGEKGEQGG GAGYGYPGVA
GPPGPPGPPG PPGPAISLDR FNRFDENSRG YQVVKGEKGE RGDRGSPGIP GTASNFDIYT
FKNELKGDQG DPGVKGEKGE PGGGYYDPRY GAPVGPPGPP GNPGLPGPKG ESIAGPPGPP
GPSGPPGVGY DGRPGPAGPP GPPGPPGNPS FSGTYRPNYP VSVPGPPGPP GPPGSPGLSS
GVTVLRSYDI LIATARQQPE GSXIYILDKA DLYLRVRDGL RQVLLGDYRT FFGDLGNEVA
EVQPPPVVVY PHAPERTSNN GAGHYSQSSA VIRPVEPPLR HPSPPVVPAA DSSESGLHLV
ALNAPQIGNM RGIRGADFLC FQQARAVGLK GTFRAFLSSR LQDLYTIVRR SDRNGFPIMN
LKNQVLFSSW ESIFSEDSNK MRENVPLYSF DGRDILRDSA WPEKMVWHGS SQKGHRQMDH
YCETWRAGEH AVTGLASSLQ SGRLLQQTPS SCSGSYIVLC IENAFTSPSK
//
