LY75_MESAU
ID LY75_MESAU Reviewed; 1722 AA.
AC Q920P9;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Lymphocyte antigen 75;
DE Short=Ly-75;
DE AltName: Full=DEC-205;
DE AltName: CD_antigen=CD205;
DE Flags: Precursor;
GN Name=LY75;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000312|EMBL:BAB69491.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=12175539; DOI=10.1016/s0304-3835(02)00067-8;
RA Maruyama K., Akiyama Y., Cheng J., Nara-Ashizawa N., Hojo T., Sasaki K.,
RA Yamaguchi K.;
RT "Hamster DEC-205, its primary structure, tissue and cellular
RT distribution.";
RL Cancer Lett. 181:223-232(2002).
CC -!- FUNCTION: Acts as an endocytic receptor to direct captured antigens
CC from the extracellular space to a specialized antigen-processing
CC compartment. Causes reduced proliferation of B lymphocytes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12175539}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:12175539}.
CC -!- TISSUE SPECIFICITY: Expressed in the thymus and cultured bone marrow
CC cells. {ECO:0000269|PubMed:12175539}.
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DR EMBL; AB059273; BAB69491.1; -; mRNA.
DR RefSeq; NP_001268813.1; NM_001281884.1.
DR AlphaFoldDB; Q920P9; -.
DR SMR; Q920P9; -.
DR STRING; 10036.XP_005069054.1; -.
DR PRIDE; Q920P9; -.
DR GeneID; 101830769; -.
DR CTD; 4065; -.
DR eggNOG; KOG4297; Eukaryota.
DR OrthoDB; 29241at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016021; C:integral component of 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; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 10.
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 Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 9.
DR SMART; SM00034; CLECT; 10.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56436; SSF56436; 10.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 9.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endocytosis; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..1722
FT /note="Lymphocyte antigen 75"
FT /id="PRO_0000017553"
FT TOPO_DOM 28..1666
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1667..1691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1692..1722
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..182
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 164..211
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 225..341
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 368..486
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 493..625
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 652..791
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 958..1091
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1110..1222
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1251..1374
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1401..1513
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1542..1661
FT /note="C-type lectin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 933
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60449"
FT MOD_RES 1703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60767"
FT MOD_RES 1719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60767"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 169..194
FT /evidence="ECO:0000250"
FT DISULFID 183..209
FT /evidence="ECO:0000250"
FT DISULFID 247..340
FT /evidence="ECO:0000250"
FT DISULFID 317..332
FT /evidence="ECO:0000250"
FT DISULFID 389..485
FT /evidence="ECO:0000250"
FT DISULFID 462..477
FT /evidence="ECO:0000250"
FT DISULFID 597..614
FT /evidence="ECO:0000250"
FT DISULFID 678..790
FT /evidence="ECO:0000250"
FT DISULFID 752..782
FT /evidence="ECO:0000250"
FT DISULFID 1060..1080
FT /evidence="ECO:0000250"
FT DISULFID 1197..1211
FT /evidence="ECO:0000250"
FT DISULFID 1488..1502
FT /evidence="ECO:0000250"
FT DISULFID 1635..1650
FT /evidence="ECO:0000250"
SQ SEQUENCE 1722 AA; 197892 MW; ACE0D451927654AF CRC64;
MGTRRVTPGC AAGLLVLLLR CFGLAEPSEF SGDDSFTIVN ENTGKCIQPL SDWIVAQDCS
ETRSMLWKWV SQHRLFHLES QKCLGLDMTK AADNLRMFRC DSSVLLWWKC EHHSLYSAAH
YRLDLKDGYA TASTNSSAVW KKGGSKENLC DQPYREIYTR DGNSYGRPCE FPFLVGETWH
HDCIRDENHS GPWCATTLNY EYDQKWGICL KPESGCEGNW EKNEQIGSCY QFNNQEVLSW
KEAYVSCQNQ GADLLSIHSA AELAYITGKE DIARIVWIGL NQLYSARGWE WSDFKPLKFL
NWDPGTPSAP MIGGSSCARM DTETGLWRSV SCEAQQPYVC KKPLNNTVEL PDVWTYSDTH
CDVGWLPQNG FCYLLANESG PWDAAHLKCK AFGGDLISIH SLADVEVVVT KLHSGDVKEE
IWTGLRNVNS PTLFQWSDGT EVTLTYWNEN EPSVPYNKTP NCVSYLGKLG QWKVQSCEKK
LRYVCKKKGE ITNDTRSDKL CPPDEGWKRH GETCYKIYEN EVPFGTNCNL TITSRFEQEF
LNDMMKKYDK SFQKYFWTGL RDADARGEYS WAATGGLKQA MTFSNWNFLQ PASPGGCVAM
STGKTLGRWE VKSCRSFRAL SICKKMSGPQ EPEEATPKPD EPCPEGWHTF PSNLSCYKVF
HIERTVRRRT WEEAERFCQA LGAHLPSFSH MNEVKEFLHL LQDQFSVQRW LWIGLNKRSP
DLQGSWQWSD RTPVSTVIMH REFQQDYDVR DCAAIKVLDN AWLRTWYYYD ERKFGYLKPF
SCDAKLDWVC QIPKGSTLQV PDWYNPERTG IHGPPVIIDG SEYWFVEEPR LNYEEAVLYC
ASNHSFLATI TTFTKLKAIR GKMENLSGEE QKWWVKANAN PIDHYFLRTR PLWHRFSMLL
DEECLQMSAK MWHLDLNKRA DCNDKLPFVC EKYNVSSLEK YSPDSAAKVQ CTGKWIPFQN
KCFLKVKSEP VTFSQASSTC HTYGGTLPSV LSKSEQDFII SLLPEMETSL WIGLRWTAYD
RISKWTDGRN LTYSNFHPLL VGRRLSIAAY FIDEESHYHC ALMLNLRKSP LTGTWNFTSC
SERHSLSLCQ KYSENEDGRP WETNSETVKY LNNLYKIISK PLTWHGALKE CLNENMRLVS
ITDPYQQAFL SVQATLRNTS FWIGLSSQDD ELNFGWSDGT YLHFSNWAVD NEKLDDCVIL
DTDGFWKTAD CDENQPGAIC YYPGNETSKE VRPLNSAKCP SPAQSTPWVP FQNSCYNFMI
TKNRHRTITQ KEVHSLCQKL HSKAQILSIR NEEENNFVVE QLLYFNYIAS WVMLGVTYEN
NSLMWFDKTA LSYTHWRAGR PAVKNHKFLA GLSTDGFWDI QSFNVIDETL HFYQHSILAC
KIEMVDYKEE RNSTLPEFIP YEDGVYNVIQ KRVTWYQALS MCSQSGRHLA SVHNPKEQLF
LEDIVNRDGF PLWVGLSSHD GSESSFEWSD GSAFDYIPWK SQGSPGNCVI LDPKGTWKHE
NCLSVKDGAI CYKPTKFKEL ASHAHSSKCP LVKRNGSQWV QYGDHCYSAE QALHTFAEAK
KLCQELDHSA TVVTIADENE NKFVSRLMRE NYNITMRVWL GLSQHSLDQS WSWLDGLDVT
FVKWENKSKN GDGKCSILIA SNETWKKVEC SRGYARVVCK VPLSPDYRGI AVLFAVLSVL
ALISGLIWFL VQRNHFRWTG LSSVRYEHGA NEDEVMLPSF HD
