ID A0A4X2KT78_VOMUR Unreviewed; 1422 AA.
AC A0A4X2KT78;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Mannose receptor C type 2 {ECO:0000313|Ensembl:ENSVURP00010012317.1};
GN Name=MRC2 {ECO:0000313|Ensembl:ENSVURP00010012317.1};
OS Vombatus ursinus (Common wombat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010012317.1, ECO:0000313|Proteomes:UP000314987};
RN [1] {ECO:0000313|Proteomes:UP000314987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yazar S.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSVURP00010012317.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 29139.ENSVURP00010012317; -.
DR Ensembl; ENSVURT00010014023.1; ENSVURP00010012317.1; ENSVURG00010009522.1.
DR GeneTree; ENSGT01050000244842; -.
DR OMA; GFIWEHI; -.
DR Proteomes; UP000314987; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 7.
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 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; 2.
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 Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000314987};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021442954"
FT TRANSMEM 1357..1379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..247
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 261..377
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 395..460
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 483..590
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 633..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 935..1054
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1088..1193
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1225..1336
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1390..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 204..230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 218..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1422 AA; 160512 MW; 997FBC1F047BD662 CRC64;
MWLPWLAPAP WRHLLRCALF LGSVVFSPSG SWISPAGAAT VATPAVPTVA PTEPNVFLIF
THGLQGCLEA QEGQVKVTPV CNTSLPAQQW KWVSRNRLFN LGAMQCLGLG TAWPGANATT
APSLGTYECD REALSLRWYC QTLGDQLPLY LGGQTGNTSK TVLSDRGDQT RGNQWRIYGT
DEDLCSVPYY EIYTIQGNSH GKPCTIPFKY DNQWFHGCTS TGREDGHLWC ATTQDYGKDE
RWGFCPIKSN DCETFWDRDQ LTNSCYQFNF QSTLSWREAW ASCEQQGADL LSITEIHEQT
YINGLLTGYS STLWIGLNDL DTNGGWQWSD NSPLKYLNWE SDQPDNPSEE NCGVIRTESS
GGWQNRDCSI ALPYVCKKKP NATVETSLQP EVEELWIGLN DLKLQMNFEW SDGSLVQFTH
WHPFEPNNFR DSLEDCVTIW GPEGRWNDSP CNQSLPSICK KAGQVSLETA EEDHGCRKGW
TWHSPSCYWL GEDYVTYSEA RRMCMDQGAT LVTITNRFEQ AYVSSLIYSW DGKYFWTALQ
DINGTGSFHW LSGDEVMYTH WNRDQPGYSR GGCVALATGS AMGLWEVKNC TTFRARYICR
QNLGTPVTPE MPGPDPTPSL TGSCPQGWAS DLKLRHCYKV FSSDRIQDKK SWPLAQSACQ
EMGAQLLSLA SYEEEHFVSN MLNKIFGESE PEIQEQHWFW IGLNRRDPRT ERSWRWSDGL
GYSYHNFDRS RHDDDDIRSC AVLDLASLQW VAMQCETQLD WICKLPKGVD VKEPDVSPQG
RKEWIRFQEA EYKFFEHHST WGQAQRICTW FQAELVSVHS QAELDFLGHS LQKFSRGQEQ
HWWIGLHTSE NDGRFRWSDK SIINFISWAP GKPRPIGKDK KCVYITASRE DWGDQRCLTA
LPYICKRSNN TSEKPPLDPP LSLLPGGCPT GWSQFINMCF RIQGHDPAER VKWSEAQRMC
EQQGAQLATI ANPLEQAFIT ASLLNVTFDL WIGLHATQKE FQWVGQEPML FGNWAPGEPS
GHSDSTSGEK LTNCVVIGHS SSPHFTGRWD DRNCLEETHG FICQRGTDTA LNPSPDALPP
APGTELSYHN SIFRLLQKPL RWHDALLLCE SLNTSLAEVD NPYTQAFLTQ ATRSLHTPLW
IGLSDEEGSR RYSWVLDELS YANWKDREPQ LPGGCGYLDV DGTWRTASCD TKLQGAVCGV
RRGFQLPRKV SHCPHALADS AWIPFREHCY SFHMELMLGH KEALQRCQKA GGAILSIMDE
MENVFVWEHM QSTEGQSGGA WLGMNFNPKG GTLVWHDNTA VNYSNWGPPG LGPSMLSHNS
CYWIQSSSGL WRPGGCTNIT MGVVCKLPQA LQENTTALVV VVLAALALLV LLAVAALLYK
RRRNPDRGAF ESARYSRSSS GPGEVAEKNI LVSDMEMNEQ QD
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