ID M3ZJ81_XIPMA Unreviewed; 1439 AA.
AC M3ZJ81;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Mannose receptor C-type 1 {ECO:0000313|Ensembl:ENSXMAP00000002273.2};
GN Name=MRC1 {ECO:0000313|Ensembl:ENSXMAP00000002273.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000002273.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000002273.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000002273.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 8083.ENSXMAP00000002273; -.
DR Ensembl; ENSXMAT00000002278.2; ENSXMAP00000002273.2; ENSXMAG00000002252.2.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; M3ZJ81; -.
DR OMA; WIDKWRV; -.
DR OrthoDB; 4271106at2759; -.
DR Proteomes; UP000002852; 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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 8.
DR CDD; cd00062; FN2; 1.
DR CDD; cd12087; TM_EGFR-like; 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:SF104; MACROPHAGE MANNOSE RECEPTOR 1; 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:UP000002852};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1439
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017222353"
FT TRANSMEM 1372..1394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..214
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 230..341
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 366..483
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 509..624
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 653..770
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 798..917
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 944..1070
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1092..1202
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1231..1345
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 171..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 185..212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1439 AA; 163658 MW; E0DBB282B5FF4FA8 CRC64;
MSPLSTFALT LCLLKALHIK ADIDSGIFLI FNQDHNKCIK VESASSVTLA QCNPRATEQQ
FRWVSESRLL SLSLKLCLGA TEIKDLVKVL LFECDENNNL QHWQCKNETL FGLKDQDLHL
NWGNFKEKNV IIYKGSGAWS RWRIFGTLGD LCSKGFQETI TIRGNAFGAP CQFPFKFASK
WYAECTTDGR TDGQLWCATE KDYDTQRKFG FCPNKGSFGW DTDPVTRVQY QRNTQATLTW
HQARMSCQQQ GADLLSIVEL HEQSYISGLT NHLGASLWIG LNSLDFESGW QWSNGNPFRY
LNWAPGHPSS VPGDSCATLN TRKASKWESS ACSKKLGYIC GKGNSTSLPP PPDKGPSFCP
SHWVPYGGQC YYLERSKKTW RDALAACHKE EADLASISNI EEQSFIITQS GYLQTDVLWI
GLNDQRNPML FEWSDHSHVT FTNWQSDEPS HAINHQEDCV LIRGKDGKWA DHMCEKTYGY
ICKKKASTKP TGGTQEEINT GCKLGTTRFG SFCYEIGRET KTFAEAMQAC SKGGSNLVDI
ADRYENAFLI SLVGLRPEKY FWTGMSNTED RNIFKWTTRR KVTFTHFNVG MPDRKQGCVA
MTTGTFAGLW DVISCSNKEK YICKKKAEGV LATTVRPTTP PLTCASGWTP VAKRNVCYKV
YKKMKENKKT WQEAQDFCKA IGGNLISILS IRDLDNMNVY STDAVWIGLR HMGPNQGFVW
SDGSPFSFES WGYGEPNNHN DNEQCAEAQF YYGHHWNDRN CDFYNDWICQ IPKGVTPKPV
PVFIVEVFNT TEDGWLIYND SHYHINKNKL SMEAARDYCK KNFGELAVIT AESERKFLWK
QLSRRSEAQQ NTQYYIGLVV NLDQSFSWVD GTPVTYTAWE NNEPNFANND ENCVTMYTSM
GYWNDINCGL ELPSICKRRG SFINTTMAPT TPPKGGCAPE WLTFKGKCYK FFADKKNWKD
ARTHCQKEGG NLVSITSEKE QAFLTTQMLS QKEDLWLGMN DINWEMNFVW TDGRAILFTN
WAKGHPTSTP DGRYFLDEVF DCVIMVGSTL KIKGQWKVED CGEKRNFVCK KNVDSQIVVP
ATTVSPKSFY KIGNDSYKLV AQKMRWDEAR RQCQADDSEL ASILNPMIQA FVTLQISTLK
EPVWIGLNNN VTGGRFKWVD NWLLSYTKWG KNEPKNHGCV YIDIDNTWKT TECSSTYYSI
CKRSQDLAPT EPPQLPGNCP EPKKDRSWMP FRGHCYYFLA SVVENWAHAS VECIKLGASL
VSIQDPIEAE FIQKNIESLQ DEAKTFWIGL YKSRDNEWMW IDNSVVDYTN WKIGMPKSDS
CVNIHSDSGE WSTNSCSRYR SYICKRPKAI PPTSRPQFVV QTVKKASSHG SAGITVAIVL
IVIAIVGLVA FLLFRKRIRL PMTTLAECTF DNKLYFNNPN RVPVDTKGLV VNIEQNEQA
//
