ID A0A665USI8_ECHNA Unreviewed; 1458 AA.
AC A0A665USI8;
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 2 {ECO:0000313|Ensembl:ENSENLP00000022663.1};
GN Name=mrc2 {ECO:0000313|Ensembl:ENSENLP00000022663.1};
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:ENSENLP00000022663.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000022663.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00479}.
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DR Ensembl; ENSENLT00000023426.1; ENSENLP00000022663.1; ENSENLG00000009082.1.
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; 7.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR CDD; cd12087; TM_EGFR-like; 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; IPR033989; CD209-like_CTLD.
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 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; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1391..1415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..234
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..506
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 528..635
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 678..804
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 823..942
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 970..1093
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1123..1228
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1261..1373
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 649..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 191..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1458 AA; 165838 MW; B66AA4787C5B821E CRC64;
MQSNDRHRNQ ESRAAWTNRQ LGLYKCTLYL FIFSVELKRS LSAAVDSDAF AFFHEGSRGC
LGVRDHSLIL SASCEEANQR WKWVTRGRLF NLGSSLCLGV TTSNFTSRLE RSPLGVYTCD
REPPRVRWTW NCGQVLENLN NYLPSPSRWN SSSTPPPSKL KWTLHGGAQD LCAKMYQEIY
TIQGNSHGRP CYLPFLYDGQ WFHSCTSIGR EDGHLWCATT YDYGKDERWG FFPLTSCSGC
ETFWDTDPLT DSCYQFNFQA TLSWSEARIS CQQQGADLLS ITKLHEQTYI NGLLTAYSAS
LWIGLNDLDI NGGWQWADSS PLKYLNWEPD HPNHAEEENC AVIKSESSGR WQNRDCSVAL
PYVCKKRPNA TLDPFTTDSW ADDEKYECDV GWQAFQAGCY KLTSEKTDWD TAQKTCQKME
ANLVSIHTLP ELEFIMHIDQ LWIGLHDTDM QMDFQWTDHT PVIFTYWHPF EPNNFRNTPE
DCVSIWGSEG RWDDSPCNLT LPSICKKPGT KSDGKPQHQD CKQGWKWHSP ACYWVGEDLL
TFDEARKACE GHGAALITIT NRFEQAYANS LLFGRSGDSF WIGLHDHPSP GSFHWLSGDE
VSFTNWNRDQ PVKVHGGCVS MATGFATGLW EVRECASAKA KFICRQNQDT SLSPEPPVPQ
PTPSLTGSCP SGWKSNSNLR YCYKVFHSSR LEQKLSWLQA HLFCQKHGAN LLSISGPDEE
YFVLQILHEA FGESEDHEQH WFWIGLNRRN PTDNGSWRWS DGLAFTYQNF GRYYYNIRQC
AAADLGTMTW LAMHCDSELD WICKLPRGTT MMHCAGSPEW IAFQEAEYKF FDHRTTWDQA
RRICSWFDSS LASVHSAEEE AFLANTLHKM VKVEGDNWWL GLYTYENDGR FRWSDNSVLN
YVSWALGRPH PLSRDRKCIH ISASKADWAD QKCHSDLPYI CKRVNVTGTI PPTPSTPHQP
AGCPDGWASY QHKCFRVFDQ SHRVTWSAAK LKCEPQGGAL AVVSNHLEQA FITTLLNNAS
VDLWVGLTSD SKGHFQWAKT SLLSYTNWAP GEPLDNSGPH HNKTRVLTTP TYRHSCHVLS
SKNTGMWASR ACEMESNGYI CQRHQGVMSV ITTASFALKP VELGGVTYRV VEKRLDWTGA
LHLCESLNGT LATVKDPYQQ AYLTLLINSL RRPAWIALYN YGGRSFTWLG EEEVSYSNWK
YGEPNQMAGC GHMTTTGQWT MTPCDAKLEA AICQISGMTV HQWIYPGHCP SLLGEWAWVP
FRNHCYAFNL QRLKLQQDAR VSCKKVGAEL LSILDETENG FVLEHIQSYE EQAHGAWLGI
SVKGRGLVWS EDIEMSYTNW EAHNLAFSVL SPNSCFWIQS NSGLWKPGSC RNRTHGVICK
RPRSKSDGDH LPTLIVVIVT GLVLVMLIVG VIYLYRRRTV GSRGSYEGAR YSRTNSSLTE
QTEKNILVSD MELNEQPE
//
