ID A0A3B4FZP0_9CICH Unreviewed; 1395 AA.
AC A0A3B4FZP0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Mannose receptor C type 2 {ECO:0000313|Ensembl:ENSPNYP00000016100.1};
GN Name=MRC2 {ECO:0000313|Ensembl:ENSPNYP00000016100.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000016100.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000016100.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 303518.ENSPNYP00000016100; -.
DR Ensembl; ENSPNYT00000016504.1; ENSPNYP00000016100.1; ENSPNYG00000012026.1.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000261460; 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; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 1328..1352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..182
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 196..312
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 342..458
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 480..587
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 630..756
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 779..898
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 923..1032
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1065..1170
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1203..1313
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 139..165
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 153..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1395 AA; 159234 MW; 56795929B1B54416 CRC64;
DFAFYLEGQG KCLGVQDRSL ALSAACEEPN QRWKWVTRRR LFNLGSSLCL GVIANNSSLK
LDKFPLGVYT CDREPPKVRW SWNCGQVLDN FNSYPLSDLP WNLTVGRSKW TLHGGLQDLC
SKTNQEIYTI QGNSNGRPCY LPFLYDGQWF HTCTSTGRED GHLWCATTYD YGKDELWGFC
PVKTNGCETF WDTDPVTDSC YQFNFQATLS WSEARISCRQ QGADLLSITK LHEQTYINGL
LTGYSAALWI GLNDLDISGG WQWADSSPLK YLNWEQEQPN HAEEKNCAVI RTESSGRWQN
RDCSVALPYV CKKRPNATLD PFTTDSWADD EKYECDVGWQ AFQAGCYKLT SEKTDWNTAQ
KTCQKMEANL VSIHTLPELE FIIRDLKKDT EQLWVGLHDT DMQMDFQWTD HTPVIFTYWH
PFEPNNFRNT QEDCVSMWGP EGRWDDSPCN LTLPSICKKP GTKSDGKPQH QQCKKGWKWH
SPACYWVGEE MLTFDGARKF CEDQGATLIT ITNRFEQAFA SSLVFGRSGD SFWIGLRNKG
NHGAFQWITN DEVSYTHWNR DQPANISSGC VSMATDTEAG LWDVRECASS KAKFICRQNQ
NTSVSPELPV PQPTPSLSGS CPSDWKSNSN LRYCYKVFHF SQLEQKLTWM RAHNFCRKHG
ANLLSISGPE EEQFVLQILH EAFGESEEHE QHWFWIGLNR RNPMDNGSWK WSDGLALTYQ
NFGRYYYNIR QCAAADLGSM TWLAMHCDSE LDWICKIPRG SVEKVPEITE GLSPEWIGFR
EAEYKFFDHR STWDQAQRIC SWFDSSLASV HSAEEQTFLA NTLRKMSKVE GDLWWLGLHT
YENDGRFRWS DHSVLNYVAW ALGRPLPISR DRKCICMSAN KEDWADQKCH SDLPYICKRV
NVTGTAPPTP PSPHPPSGCR DGWSSFQHKC FRVFDQSNRV TWSAAKRIQM AYTFVTTLLK
NASAELWVGL TSDSKANFKW AKAGLLSYTN WAPGEPLDNS GPHQNKTPGN CVVMYHENLQ
KKTGMWASRA CEMESHGFIC QRQQEQGLPP APALIPASLS KPVELGGVTY RVVKKRLDWT
GALHLCESLN GTLARVKDPF QQGYLTLLIN SLRQPAWIGL YNYGGRSFTW LNNEDVTYSN
WNDGEPSLMA GCGHMTTTGQ WTVTPCDSRL DAAICQMNEQ VIHQWIYPGM CPQSLGEWAW
VPFRNHCYAF NLQLLRLQDD AHRSCKKIGA ELLSIMDETE NGFVWEHIQS YAEQAHGAWL
GVSVKGLVWS EGTEMLYTNW EGHDVVSSVL SINSCFWIQS NTGRWKPGSC RNRTHGVICK
RPRNSHRLPT LIVVMVAGLV LVVLIVGMIY FYRHRTVGSR GSYEGARYSR TNSNSAEQAE
KNILVSDMEL NEQPE
//
