ID A0A3Q3N9C7_9TELE Unreviewed; 1427 AA.
AC A0A3Q3N9C7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Mannose receptor, C type 2 {ECO:0000313|Ensembl:ENSMAMP00000033022.2};
GN Name=MRC2 {ECO:0000313|Ensembl:ENSMAMP00000033022.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000033022.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000033022.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 205130.ENSMAMP00000033022; -.
DR Ensembl; ENSMAMT00000033878.2; ENSMAMP00000033022.2; ENSMAMG00000022220.2.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000261640; 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 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; 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:UP000261640};
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 1363..1384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 145..193
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 207..323
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 353..464
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 486..594
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 636..764
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 787..906
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 934..1053
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1086..1191
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1224..1336
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 607..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 150..176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 164..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1427 AA; 161650 MW; FCECDC19762FCE41 CRC64;
QAPLDSDDFA FYHEGAQGCL GVRDHSLILS ASCEENNQRW KWVTRGRLFN LGSSLCLGVT
SGNLTSRSDR SPLGVYTCDQ EPPRVRWTWN CGQVLNSLNI YLPSPSLWNS SSSSSPAKHK
WTLHGGAQDL CTKPYREIYT IQGNSHGRPC YMPFLYGGQW FHSCTSIGRE DGHLWCATTY
DYGKDERWGF CPVKSNDCET FWDINPLPDS CYQFNFQATL SWSEARISCQ QQGADLLSIT
KLHEQTYING LLTGYSASLW IGLNDLDING GWQWADSSPL KYLNWEQDQP SHAEEENCAV
IRTESSGRWQ NRDCSVALPY VCKKRPNATL DPFTTDSWAN DEKYECDVGW QAFQAGCYKL
TSEKIDWDTA QKTCQKMEAN LVSIHTLPEL EFIMHIDQLW IGLHDTNMQM DFQWTDHTPV
IFTYWHPFEP NNFRNTQEDC VSIWGSEGRW DDSPCNLTLP SICKKPGTKS DGKPQQQECK
QGWKWHSPTC YWVGEDLLTF DEARKSCEDH VATLVTITNR FEQAFVNSLV FGRSGDSFWI
GLNDQGSPGS FHWLSGDEVS YTNWNRDQPV DVRGGCVSMA TGFATGLWEV KECSSSKAKF
ICRQNQDTSL SPEPPVPQPT PSLSGSCPSG WKSNSNLRYC YKVFHSSQLE QKLSWLQAHL
FCRKHGANLL SISGPDEEHF VLQVLHEAFG WVESEDHEQH WFWIGLNRRN PMDNGSWKWS
DGLAFTYQNF GRYYYNIRQC AAADLGTMTW LAMHCDSELD WICKIPRGSA EKEPEDSEGQ
FLKWIGFQEA EYKFFDHRTT WDQAQRICSW FHSSLASVHS AEEETFLANT LHKLAKAESA
NWWLGLHTYE NDGRFRWSDH SVLNYVSWAL GSPRPLSRDR RCIQISASKA EWSDQKCHSD
LPYICKRVNV TGTIPPTPSS PHPSSGCPDG WASYQHKCFR VFDQSYKVTW SAAKLKCETQ
GGVLAVVSSH LEQAFVTTLL KNTSIDLWVS LTSDSKGHFQ WTKTGLLSYT NWAPGEPIDN
SGPHHNKTPG NCVVMIHGNP QKNAGMWASR ACEMESNGFI CQRQQDPGLP PSPALIPASL
SKPVELGGAT YRVVEKLLDW TGALHLCESL NGTLARVKDP YQQAYLTLLI NSLRRPAWIA
LYNYGGRSFT WLGEEDVSYS NWKDGEPNQM AGCGHMTTTG QWTMTPCDAK LEAAICQINE
PVAHQWTYPG QCPHSLGEWA WVPFRNHCYA FNLQNLKLQQ DARLSCKKVG AELLSVLDET
ENGFVWEHIQ SYAEQAHGAW LGITVKGRGL VWTEDTEMSY TNWEVHDAAF SVLSPNSCFW
IQSNSGLWKP GSCRNRTHGV ICKRPRSAET SAVTMDGDHL PTLIVVMVTG LVLVVLIVGF
IYFYRRQTVG SRGSYEGARY SRTSSSLAEQ AEKNILVSDM ELNEQSE
//
