ID A0A673WTE3_SALTR Unreviewed; 1472 AA.
AC A0A673WTE3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=C-type mannose receptor 2-like {ECO:0000313|Ensembl:ENSSTUP00000011381.1};
GN Name=MRC2 {ECO:0000313|Ensembl:ENSSTUP00000011381.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000011381.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000011381.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSSTUT00000012079.1; ENSSTUP00000011381.1; ENSSTUG00000004372.1.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000472277; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 7.
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 PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 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; 2.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000472277};
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..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1472
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025534079"
FT TRANSMEM 1405..1429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..235
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 249..365
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 395..508
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 530..637
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 683..807
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 837..953
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 981..1102
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1135..1240
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1275..1389
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1440..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 192..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 206..233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1472 AA; 166077 MW; A21AD32F3D59FE32 CRC64;
MESFLNSVID CPLSLSLSLS LFLSLCFSIS LSTEPVNGDV FVFFHEGAQG CLGVQGHSLS
LSKSCEDDAQ KWKWVTRGRL FNLGSSLCLG LTTGNYSSRE DVSPLGVYPC DREPPGVRWT
WYCVHVLENL NLYLPSPSHP VNPSANSSVV ASDVKPPREG LKWRLFGDDQ DLCSRSYREI
YTIQGNSQGR PCYLPFMYDG QWFHNCTSIG REDGHLWCAT TFDYGKDENW GFCPVKSNDC
ETFWDTDPLT DSCYQFNFQA TLSWSEARIS CQQQGADLLS ITKLHEQTYI NGLLTGYSAA
LWIGLNDLDI SGGWQWADSS PLKYLNWEND QPGHVDEENC AVIRTESSGR WQNRDCSVAL
PYVCKKRPNA TLDPFTTDSW ADDEKYECDV GWQAFQAGCY RLTSEKVVWD AAQKTCQKME
ANLVSLHTLP ELEFIINNIK RDVEELWIGL HDTAMQMDFQ WTDHTPVIFT YWHPFEPNNF
QNTPEDCVTI WGPVMCSHCQ QTLPSICKKA AQKTDGQAQD HGCKPGWRWH SPACYWVGEE
QVTFEEGRKA CAGSGATLIT ITNRFEQAFV NSLVFGRSGD SFWIALLDQS SPGKFHWLSG
DEVAYTNWNR DQPGNIKGGC VTMETGYATG LWEVKDCASA RAKFICRLNQ DTSLSPEPPT
PHPTPSLTGS CPNGWKTNGK LHHCYKVFDS AQMDQKLSWL QAHLACQRHH GANLLSVSGP
EEEHFILQIL HEAFGESEDH EQRWFWIGLN RRNPMDNGSW KWSDGLAYTY QNFGRYYYNV
RQCAAADLGT MTWLAMRCDY ELDWICKIPK GNSKTTEPHI DTDTVTKDTW PQGWVGFQEA
EYKFFDHRST WDQAQRICSW FGASLASIHS DMEEVFLAKT LHKVEGDHWW VGLHTYENDG
RFHWSDHSVL NYVSWALGRP HPLSRDRKCV HMSVSKAEWA DQKCHSDLPY ICKRVNVTGT
IPPTPSTPLP PAGCPDGWGP FLHKCYKVFG HEESRRATWS GAKLMCESQE GALAVVPNHV
EQAFVTTLLS NVSFDLWVGL TSDSKGHFQW ARPGLLSYTN WASGEPLDNS GPLHNKTPGN
CVVMIHGNPA KNTGMWASRA CEMEKHGYIC QKKQDPALPP GAALLPSSLS GALDLGGVSY
RIVKKRLDWM GALHVCESLN GTLASVRDPY QQAYLTLLMN SLHLPAWIGL YNYEGRRFSW
LGEEDLIYTA WRDGEPNTLS GCGHMTTGGQ WTMNPCDAKL DAAICLINTG EALVHKWSFP
GQCPHSLGDW AWVPFRNHCY SFNLQILQLQ TDAHSSCRKV GGQLLSVLDE TENGFVWEHI
QGYQEQAHGA WLGMNFNSKG GSLMWSESAE VKFTNWEVQG TNLSMLFPNA CFWIQSNTGL
WKPGSCKNRT HGVICKRPRT EEDHLPTLIV IMVTGLALVI LIVGVIYLYR RRQAGSRGSY
EGARYSRTNS NPSEQAEKNI LVSDMELNEQ PE
//
