ID V8NX67_OPHHA Unreviewed; 1363 AA.
AC V8NX67;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=C-type mannose receptor 2 {ECO:0000313|EMBL:ETE66273.1};
DE Flags: Fragment;
GN Name=Mrc2 {ECO:0000313|EMBL:ETE66273.1};
GN ORFNames=L345_07949 {ECO:0000313|EMBL:ETE66273.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE66273.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE66273.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE66273.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the true venom lectin family.
CC {ECO:0000256|ARBA:ARBA00006250}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE66273.1}.
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DR EMBL; AZIM01001608; ETE66273.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; cd03590; CLECT_DC-SIGN_like; 1.
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; 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 PANTHER; PTHR22803:SF69; C-TYPE MANNOSE RECEPTOR 2; 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; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:ETE66273.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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 1299..1320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..142
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 156..272
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 286..402
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 424..538
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 558..679
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 727..846
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 875..995
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1025..1128
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1166..1278
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1336..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 99..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 113..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE66273.1"
SQ SEQUENCE 1363 AA; 156395 MW; A37D78CC9F6EADEE CRC64;
MQCLGVSWKS ANSSATTHAL ATYECDRESI NMRWNCRSLG DQLSQYLSSR LGNWSLTPAE
RGDQAHGGQW KIYGHDEDLC SRPYSEIYTI QGNSHGKPCT IPFKYDNQWF HDCTSMGRGD
GHLWCATTQD YGEDERWGFC PIKSNDCDTF WDRDQLTNSC YQFNFQSTLS WQEAGKSCEQ
QGASLLSITA IHEQTYINGL LTGYGSTLWI GLNDLDLNGG WQWSDNSPLK FLNWENDQPD
NPNEENCGVI RTESSGGWQN RDCSIALPYI LESEVKIDCD PSWQPFQSNC YRLISEKKTW
IDAKKTCLRS EGDLVSIHTL SELEFVSKQI KQDVEELWIG LNDLRLQMNF EWSDGTPVQF
TFWHPFEPNN FRDSLEDCVT IWGPEGRWND SPCNQTLPSV CKKRGRVSQG KEEDHGCRKG
WKWHSPSCYW LGDDHVIYNE ARKMCVDFGS ALVTITNRFE QAYVSSLIYG WEDEYFWTAL
QDINETGSFL WLSGDEVTYT HWNRNQPGTY HVPNRYNKGG CVALATGSAM GLWEVKNCTT
FKAKYICRQN LGTPVFSYDK LQEKKNWITA HLFCQELKAQ LLSLSDYEEE HFVANTLNKI
FGELEPDIHE QHWFWIGLNR RSPRAEGSWS WSDGVGFSYH NFDRSNHDND DIRNCVALDL
ASLQWVPLQC EIKLDWICKL PKGDWDCNEE FDMLDGDMIC HSFIHSIGTE VAEPETTIQG
SKEWLKFQDA EYKFFDHHST WVQAQRICTW FQADLVSIHS QTELDFLGQN LKKFSRGQEE
HWWIGLNTYE NDGRFRWSDG SLLNFISWAP GKPRLINKEK KCVYMTASRE DWGDQKCLTA
LPYICKRTNI TTVQPSLPSL SVPTPGSCAQ DWHAFINKCF RIYNQEKVTW LEAKRKCEIQ
GGILATVSNH LEQAFITTLL PNVTFDIWIG LHDSKKEFLW VESETVKYVN WAPGEPSGYG
TSIANDQPTN CAVMWHGLPS LFTGRWDDRN CQEEKHIFIC QRSKDPTMNP SSTSFSSVLN
CTLLYLNNTY RVLMKPLKWH EALLLCESLN GSLANVMEPF TQAFLTQAVN SLHTPLWIGL
SNEGGRRNYE WFTDESVSYT NWQDGEPQQI VGCAYMDIDG TWRTATCNTN LQGAICKLNT
GPLSSHKWSY NGSCPKTIED SSWVPFRNHC YAFHMEVILG QKEAVKKCQK VGGMVLSIED
EMENIFIWQH LQVYESQAKG VWLGMSFNPK GGTLVWHDNT AVNYSNWGQH DTGPSMISPN
SCYWIQSSNG IWRLGSCSNV TMGVICKTTR AFLENTKTIV VVILSSLALC ALIAVALYLY
KRRWISERGT FESARYSRTN ASPSESAEKN ILVSDMEMNE QQD
//
