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Database: UniProt
Entry: A0A087YFV5_POEFO
LinkDB: A0A087YFV5_POEFO
Original site: A0A087YFV5_POEFO 
ID   A0A087YFV5_POEFO        Unreviewed;      1439 AA.
AC   A0A087YFV5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Mannose receptor C-type 1 {ECO:0000313|Ensembl:ENSPFOP00000016908.2};
GN   Name=MRC1 {ECO:0000313|Ensembl:ENSPFOP00000016908.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016908.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000016908.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   EMBL; AYCK01006252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01006253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007555723.1; XM_007555661.2.
DR   STRING; 48698.ENSPFOP00000016908; -.
DR   Ensembl; ENSPFOT00000016930.2; ENSPFOP00000016908.2; ENSPFOG00000016777.2.
DR   GeneID; 103140480; -.
DR   KEGG; pfor:103140480; -.
DR   CTD; 100286774; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT01050000244842; -.
DR   OMA; WIDKWRV; -.
DR   OrthoDB; 4271106at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00037; CLECT; 8.
DR   CDD; cd00062; FN2; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 8.
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; IPR016187; CTDL_fold.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR22803:SF104; MACROPHAGE MANNOSE RECEPTOR 1; 1.
DR   PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR   Pfam; PF00040; fn2; 1.
DR   Pfam; PF00059; Lectin_C; 8.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00013; FNTYPEII.
DR   SMART; SM00034; CLECT; 8.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 8.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1439
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001834447"
FT   TRANSMEM        1372..1394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          166..214
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          230..341
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          366..483
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          509..624
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          653..770
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          798..917
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          944..1070
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1092..1202
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1231..1345
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DISULFID        171..197
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        185..212
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ   SEQUENCE   1439 AA;  163801 MW;  D762024C33619F23 CRC64;
     MSPLSTFALI LCLLQALHIK ADIDSGIFLI FNQNHNKCIK VESASSVILA QCNPRASEQQ
     FRWVSESRLL SLSLKLCLGA TAIKDWVKVL LFECDESSSL QHWQCKNETL FGLKDQDLHL
     NWGNFKEKNV MIYKGAGEWS RWKIFGTQGD LCSKGFQETF TIRGNAFGAP CQFPFKYTSK
     WYAECTTDGR TDGQLWCATE KDYHTNTKFG FCPTKGSIGW DTDPVTRVQY QRNTQATLTW
     HQARVSCQQQ GADLLSIVEL HEQSYISGLT NHLGTSLWIG LNSLDFESGW QWSNGNPFRY
     LNWAPGNPSS VPGESCAILN TRKASKWESS ICSKKLGYIC RKGNSTSLPP PPDKGPSFCP
     SHWVPYGGQC YYLERSKKMW RDALAACHKE EADLASISNI EEQSFIITQS GYLQTDVLWI
     GLNDQRNPML FEWSDRSHVT FTNWQSDEPS HATNHQEDCV LIRGKEGKWA DHMCEKTYGY
     ICKKKASTKP TGGTQEEVNP GCKLGTTRFG SYCYEIGRET KSFEEAMQAC SKGGSNLVDI
     ADRYENAFLI SLVGLRPERY FWTGLTNTEE INVFKWTTRR QVTFTHFNVG MPDRKQGCVA
     MTTGTFAGLW DVISCSNKEK YICKKKAEGV LATTVQPTTP QLSCASGWTP VAKRNVCYKV
     YKKMKENKKT WQEAQDFCKA IGGNLISLLS MRDLDNVNFY SSDPVWIGLR VMGPNQGFVW
     SDGSPFSFEN WGFGEPNNHN DNEHCAEVHF HYSRHWNDRN CDSYNDWICQ IRKGVTPKPE
     PVFVVEVFNT TEDGWLIYND SHYYINKNKL PMEAARDYCK KNFGELAVIT GESERKFLWK
     HLTRDPQAQN HAQYYIGLIV NLDQSFSWVD GTPVTYTAWE NNEPNFANND ENCVTMYSSM
     GYWNDINCGL ELPSICKRRG SFINTTMAPT TPPKGGCAPE WLNFKGKCYK FFADKKNWKD
     ARTHCQKEGG NLVSITSERE QAFLTTQMLS QKEDLWLGMN DINWEMHFVW TDGKAISFTN
     WAKGHPISTP DGRFFLDEVF DCVIMVGSIL KIKGQWKVED CSEKRGFVCK KNVDSQIAVP
     ATTVSPKSFY KIGNDSYKVV AQKMRWDEAR RQCQADDSEL ASILNPMIQA FVTLQISTLK
     EPVWIGLNNN VTGGRFKWVD NWLLSYTKWG KNEPKNYGCV YIDVDHTWKT AECSSTYYSI
     CKRSQDLAPT EPPQLPGNCP EPKKDRSWMP FRGHCYYFVG SVVDNWAHAS VECMKLGASL
     VSIQDPVEAK FIQKNIESLQ DETKSFWIGL YKSHDDEWMW IDNSVVDYTN WIIGMPKSDS
     CVNIHSDSGK WSTNSCSRYR SYICKRPKVI PPTSKPQFVV QTVKEASLHG SAGITVAIVL
     IVIAIVGLAA FLLFRKRIRL PMATLAECTF DNKLYFNNPN RVPVDTKGLV VNIEQNEQA
//
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