ID A0A665X1Y7_ECHNA Unreviewed; 1437 AA.
AC A0A665X1Y7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Mannose receptor C-type 1 {ECO:0000313|Ensembl:ENSENLP00000050089.1};
GN Name=mrc1 {ECO:0000313|Ensembl:ENSENLP00000050089.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000050089.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000050089.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSENLT00000051310.1; ENSENLP00000050089.1; ENSENLG00000020475.1.
DR InParanoid; A0A665X1Y7; -.
DR OMA; WIDKWRV; -.
DR OrthoDB; 4271106at2759; -.
DR Proteomes; UP000472264; Unplaced.
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 CDD; cd00161; RICIN; 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: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 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; 4.
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:UP000472264};
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..1437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025569734"
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 225..341
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 367..484
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 510..625
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 654..771
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 799..914
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 941..1070
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1092..1203
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1232..1346
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 1437 AA; 161968 MW; BA60A8BFB1767B9C CRC64;
MLPCSHLAVI LCLLQVLHIT ANTDSGSFLI YNENHNKCIK VESATSVTVA LCDPHAKQQQ
FRWASESRVL SLSLKLCLAA TEIKDWVKVI LTECDENSDL QHWQCKNETL FGLKDQDLHL
NWGNRNERNI MIYKGSGLWS RWRIFGTRGD LCSKGYQEIF TIGGNSFGVP CQFPFKFGET
WFAECTKEGR TDGQLWCATE RDYDKTKKWG FCPTQISSGW DTDPVTGVQY QRNAQSVLTW
HQARRSCQQQ GADLLSIVEL HEQSYISGLT NNLGTSLWIG LNSLDFESGW QWSNGNPFRY
LNWAPGHPSS EPGLTCATLN AAKASKWESI SCNKKLGYIC RKGNSTSLPP PPSKDQPSFC
PNHWVPYAGS CYYLERNKLM WRDALAACHK EGADLASIHN IEEQSFIITQ SGYLPTDVLW
IGLNDRRNQM LFEWSDHSHV TFTVWKGDEP SHATNLQEDC VLITGKDGKW ADHMCEKTYG
YICKKKASIK PSEGAREEAN PGCKLGSIRF GSHCYTIGAE AKTFNEAKQA CSQSGSNLVD
VVDRYENAFL VSLVGLRPEK YFWTGFSNTE DRTTFQWTTK RKVTFTHFNV GMPGREQGCV
AMTTGKFAGL WDVVSCSNKE KYICKKRAEG VQVTTVPPTT PALSCASGWT PAGNRDVCYK
LYKKNGDLKK NWQEAQDFCK AIGGDLMSIH SMQDLHNAPF RGSDAAWIGF TSMDTSKGFV
WTDGSANGFE NWGFGEPNNY NDNEHCAEVQ FYYGRHWNDR HCEAYNDWLC QIRKGVTPKP
EPAVVVTVYN TTEDGWIIYN DTQYFINNDN LPMEAARAYC KANFAELAVI TGESERKFIW
KQIVKGTEGQ YYIGMVVNLD KSFSWVDGTP ISYTAWEHNE PNFANNDENC VTVLKSMGYW
NDINCGMELP SVCKRSNSFV NTTIAPTTVS KGGCAPEWVA FEGRCYKFVV GNDKKNWQDA
RTSCINQGGN LVSIVNEREQ AFLTTQTLNY NGDIWIGMND VNWEMHFVWT DGKGISFTNW
AKGHPTSVPE GRFSLSDEMY DCVIMVGGSS KISGSWKVDD CYSKQSFVCK RNPDSQIAVP
PTTVLPKAFN KFGNDSYKLV AQKMRWDEAR RQCQADDADL VSILNPVTQA YIILQISKHN
QPVWLGLNSN VTGGRYKWVD NWLLSFTKWG KDEPKSNYGC VYIDVDKTWK TAPCTNTYYS
ICKRSSVIAP TEPPQLPGNC PEPKKRKTWI PFRGHCYSFL GSFVDNWAHA SVECLKMGAS
LVSIEDPHES QFIQKNLELL QDGAKSFWIG LYKNHDGEWM WIDNSVVDYT NWKWGMPKSD
SCVDINSDSG QWSTTSCSRF RSYICKTPKL IAPTEKPPSV AHIVEEVSHG SAGITVAVVL
VIIAILGLGA FLLFRKQIPT PALGECNFDN KLYFNNPIRA PVDTKGLVAN IEQNEQA
//
