GenomeNet

Database: UniProt
Entry: A0A3P9PGD1_POERE
LinkDB: A0A3P9PGD1_POERE
Original site: A0A3P9PGD1_POERE 
ID   A0A3P9PGD1_POERE        Unreviewed;       761 AA.
AC   A0A3P9PGD1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Collectin-12 {ECO:0000256|ARBA:ARBA00017460};
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:ENSPREP00000020897.1, 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:ENSPREP00000020897.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000020897.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_008432704.1; XM_008434482.2.
DR   AlphaFoldDB; A0A3P9PGD1; -.
DR   STRING; 8081.ENSPREP00000020897; -.
DR   Ensembl; ENSPRET00000021118.1; ENSPREP00000020897.1; ENSPREG00000014130.1.
DR   GeneID; 103479820; -.
DR   KEGG; pret:103479820; -.
DR   CTD; 81035; -.
DR   GeneTree; ENSGT00950000183074; -.
DR   OMA; KAMNTNT; -.
DR   OrthoDB; 4613106at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000014130; Expressed in head and 1 other cell type or tissue.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033989; CD209-like_CTLD.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR016187; CTDL_fold.
DR   PANTHER; PTHR22803:SF146; COLLECTIN-12; 1.
DR   PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          633..751
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          434..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          72..124
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          216..250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          370..404
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        555..575
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  82142 MW;  4841206BE06F5496 CRC64;
     MKDEFTDEEE VQSFGYKRFG IQEGTECTKC KNDWALRAAI ALLYVLCALL TIAVAVLGYK
     VVQRMDNVTE GMQNYGGKIN AVETDLKKLD DQAGEKSLNA TSEISTFKSD LEGLQNQLKD
     ISSRATSNRD MLEDLLVTGD NMQNGHVSLQ SVLDGNADSL RGINQSLASY SGMIDHLQAD
     TARLQSELQE QVKVQSETQV NVNSLNITQG QQRNLLGLLQ KTVEDVSQAV QKLKNDYQIL
     QQTANHTRSD SQWLKEKVQN LQVLAANNSA LASSNGDTLD DLRTQLNALV IQIQNTSAIT
     ESHDQGLREL MDRQRDNDNT TSLKFDEMEV RLDKHENAMD RVTGNMSFAT QILGVISSDL
     TGLRSCAETV MRHTDLLADL NATMEEAKTN SKDLRTQQDE LATRLDQEVN NLSNVMQEMK
     LIDSKHSQLI TNFTILQGPP GPKGSRGDKG PQGPMGQTGH KGDKGDKGIP GLLGPKGDRG
     PTGPAGGTGP KGSTGAQGLP GPKGSRGSGG RPGSPGEKGD PGSNGYPGTN GNPGLPGPQG
     PQGLRGAAGP PGLEGPRGPV GPIGPAGPPG LPGLPGPVSS VNIKPTRAPQ VIKPPLPTLP
     SVPTEKSQDS AQEQPSAAAS TPAPGCPPEF RKFGDSCYYF SSGTQRLNFN EANKFCKNIS
     SHMLIINDNE EQQFIRNAIS KGYFWLGLTD KEEENVWKWV DGTIPVFTNW KPGQPDNWTH
     GHVNGEDCAG LIHNANWNDF YCTDRIGFIC ERSSELVVPV L
//
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