ID A0A665X2H4_ECHNA Unreviewed; 1400 AA.
AC A0A665X2H4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Mannose receptor C-type 1 {ECO:0000313|Ensembl:ENSENLP00000050132.1};
GN Name=mrc1 {ECO:0000313|Ensembl:ENSENLP00000050132.1};
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:ENSENLP00000050132.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000050132.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSENLT00000051365.1; ENSENLP00000050132.1; ENSENLG00000020475.1.
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; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1335..1357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..199
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 210..326
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 352..469
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 495..608
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 637..753
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 781..896
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 923..1052
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1074..1185
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1226..1315
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 156..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 170..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1400 AA; 157589 MW; 721B8AF67B084E2C CRC64;
LVLFSSASDS GSFLIYNENH NKCIKVESAT SVTVALCDPH AKQQQFRWAS ESRVLSLSLK
LCLAATEIKD WVKVILTECD ENSDLQHWQC KNETLFGLKD QDLHLNWGNR NERNIMIYKG
SGLWSRWRIF GTRGDLCSKG YQEIFTIGGN SFGVPCQFPF KFGETWFAEC TKEGRTDGQL
WCATERDYDK TKKWGFCPTQ ISSGWDTDPV TGVQYQRNAQ SVLTWHQARR SCQQQGADLL
SIVELHEQSY ISGLTNNLGT SLWIGLNSLD FESGWQWSNG NPFRYLNWAP GHPSSEPGLT
CATLNAAKAS KWESISCNKK LGYICRKGNS TSLPPPPSKD QPSFCPNHWV PYAGSCYYLE
RNKLMWRDAL AACHKEGADL ASIHNIEEQS FIITQSGYLP TDVLWIGLND RRNQMLFEWS
DHSHVTFTVW KGDEPSHATN LQEDCVLITG KDGKWADHMC EKTYGYICKK KASIKPSEGA
REEANPGCKL GSIRFGSHCY TIGAEAKTFN EAKQACSQSG SNLVDVVDRY ENAFLVSLVG
LRPEKYFWTG FSNTEDRTTF QWTTKRKVTF THFNVGMPEQ GCVAMTTGKF AGLWDVVSCS
NKEKYICKKR AEGVQVTTVP PTTPALSCAS GWTPAGNRDV CYKLYKKNGD LKKNWQEAQD
FCKAIGGDLM SIHSMQDLHN APFRGSDAAW IGFTSMDTSK GFVWTDGSNG FENWGFGEPN
NYNDNEHCAE VQFYYGRHWN DRHCEAYNDW LCQIRKGVTP KPEPAVVVTV YNTTEDGWII
YNDTQYFINN DNLPMEAARA YCKANFAELA VITGESERKF IWKQIVKGTE GQYYIGMVVN
LDKSFSWVDG TPISYTAWEH NEPNFANNDE NCVTVLKSMG YWNDINCGME LPSVCKRSNS
FVNTTIAPTT VSKGGCAPEW VAFEGRCYKF VVGNDKKNWQ DARTSCINQG GNLVSIVNER
EQAFLTTQTL NYNGDIWIGM NDVNWEMHFV WTDGKGISFT NWAKGHPTSV PEGRFSLSDE
MYDCVIMVGG SSKISGSWKV DDCYSKQSFV CKRNPDSQIA VPPTTVLPKA FNKFGNDSYK
LVAQKMRWDE ARRQCQADDA DLVSILNPVT QAYIILQISK HNQPVWLGLN SNVTGGRYKW
VDNWLLSFTK WGKDEPKSNY GCVYIDVDKT WKTAPCTNTY YSICKRSSGQ TIPPSVVKPG
YLSGATVIPS SGHFENFHLP LWLCLSGASL VSIEDPHESQ FIQKNLELLQ DGAKSFWIGL
YKNHDGEWMW IDNSVVDYTN WKWGMPKSDS CVDINSDSGQ WSTTSCSRFR SYICKTPKLI
APTEKPPSVV SHGSAGITVA VVLVIIAILG LGAFLLFRKQ IPTPALGECN FDNKLYFNNP
IRAPVDTKGL VANIEQNEQA
//
