LY75_MOUSE
ID LY75_MOUSE Reviewed; 1723 AA.
AC Q60767; B2RWW5; Q8C7T3; Q91XL8; Q9QUZ6;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 168.
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; Synonyms=Cd205;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAA80215.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP AND GLYCOSYLATION.
RC STRAIN=BALB/cJ; TISSUE=Dendritic cell, and Thymus;
RX PubMed=7753172; DOI=10.1038/375151a0;
RA Jiang W., Swiggard W.J., Heufler C., Peng M., Mirza A., Steinman R.M.,
RA Nussenzweig M.C.;
RT "The receptor DEC-205 expressed by dendritic cells and thymic epithelial
RT cells is involved in antigen processing.";
RL Nature 375:151-155(1995).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Park C.G., Steinman R.M.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-485.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 28-52, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=7553896; DOI=10.1006/cimm.1995.1218;
RA Swiggard W.J., Mirza A., Nussenzweig M.C., Steinman R.M.;
RT "DEC-205, a 205-kDa protein abundant on mouse dendritic cells and thymic
RT epithelium that is detected by the monoclonal antibody NLDC-145:
RT purification, characterization, and N-terminal amino acid sequence.";
RL Cell. Immunol. 165:302-311(1995).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-865.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-529; ASN-865; ASN-1077 AND
RP ASN-1104.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1704 AND SER-1720, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:7553896}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:7553896}.
CC -!- TISSUE SPECIFICITY: Expressed in dendritic and thymic epithelial cells
CC and lymph nodes. {ECO:0000269|PubMed:7553896,
CC ECO:0000269|PubMed:7753172}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19349973,
CC ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:7553896,
CC ECO:0000269|PubMed:7753172}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=DEC-205;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_180";
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DR EMBL; U19271; AAA80215.1; -; mRNA.
DR EMBL; AF395445; AAK81722.1; -; mRNA.
DR EMBL; AK049301; BAC33668.1; -; mRNA.
DR EMBL; BC150734; AAI50735.1; -; mRNA.
DR CCDS; CCDS38126.1; -.
DR PIR; S58880; S58880.
DR RefSeq; NP_038853.2; NM_013825.3.
DR AlphaFoldDB; Q60767; -.
DR SMR; Q60767; -.
DR BioGRID; 201246; 1.
DR STRING; 10090.ENSMUSP00000108152; -.
DR GlyConnect; 2488; 1 N-Linked glycan (1 site).
DR GlyGen; Q60767; 14 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q60767; -.
DR PhosphoSitePlus; Q60767; -.
DR EPD; Q60767; -.
DR MaxQB; Q60767; -.
DR PaxDb; Q60767; -.
DR PeptideAtlas; Q60767; -.
DR PRIDE; Q60767; -.
DR ProteomicsDB; 295733; -.
DR DNASU; 17076; -.
DR Ensembl; ENSMUST00000028362; ENSMUSP00000028362; ENSMUSG00000026980.
DR GeneID; 17076; -.
DR KEGG; mmu:17076; -.
DR UCSC; uc008jud.1; mouse.
DR CTD; 4065; -.
DR MGI; MGI:106662; Ly75.
DR VEuPathDB; HostDB:ENSMUSG00000026980; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; Q60767; -.
DR OMA; KTADCND; -.
DR OrthoDB; 29241at2759; -.
DR BioGRID-ORCS; 17076; 7 hits in 74 CRISPR screens.
DR PRO; PR:Q60767; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60767; protein.
DR Bgee; ENSMUSG00000026980; Expressed in brain blood vessel and 108 other tissues.
DR ExpressionAtlas; Q60767; baseline and differential.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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:0038023; F:signaling receptor activity; IBA:GO_Central.
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; 2.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endocytosis; Glycoprotein;
KW Lectin; Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:7553896,
FT ECO:0000269|PubMed:7753172"
FT CHAIN 28..1723
FT /note="Lymphocyte antigen 75"
FT /id="PRO_0000017554"
FT TOPO_DOM 28..1667
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1668..1692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1693..1723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..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 959..1092
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1111..1223
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1252..1375
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1402..1514
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1543..1662
FT /note="C-type lectin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 934
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60449"
FT MOD_RES 1704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000269|PubMed:19349973"
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:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 1104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 1226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1627
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 1061..1081
FT /evidence="ECO:0000250"
FT DISULFID 1198..1212
FT /evidence="ECO:0000250"
FT DISULFID 1489..1503
FT /evidence="ECO:0000250"
FT DISULFID 1636..1651
FT /evidence="ECO:0000250"
FT CONFLICT 51
FT /note="S -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1283
FT /note="S -> P (in Ref. 1; AAA80215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1723 AA; 197352 MW; 5FACCFE712C08B1C CRC64;
MRTGRVTPGL AAGLLLLLLR SFGLVEPSES SGNDPFTIVH ENTGKCIQPL SDWVVAQDCS
GTNNMLWKWV SQHRLFHLES QKCLGLDITK ATDNLRMFSC DSTVMLWWKC EHHSLYTAAQ
YRLALKDGYA VANTNTSDVW KKGGSEENLC AQPYHEIYTR DGNSYGRPCE FPFLIGETWY
HDCIHDEDHS GPWCATTLSY EYDQKWGICL LPESGCEGNW EKNEQIGSCY QFNNQEILSW
KEAYVSCQNQ GADLLSIHSA AELAYITGKE DIARLVWLGL NQLYSARGWE WSDFRPLKFL
NWDPGTPVAP VIGGSSCARM DTESGLWQSV SCESQQPYVC KKPLNNTLEL PDVWTYTDTH
CHVGWLPNNG FCYLLANESS SWDAAHLKCK AFGADLISMH SLADVEVVVT KLHNGDVKKE
IWTGLKNTNS PALFQWSDGT EVTLTYWNEN EPSVPFNKTP NCVSYLGKLG QWKVQSCEKK
LRYVCKKKGE ITKDAESDKL CPPDEGWKRH GETCYKIYEK EAPFGTNCNL TITSRFEQEF
LNYMMKNYDK SLRKYFWTGL RDPDSRGEYS WAVAQGVKQA VTFSNWNFLE PASPGGCVAM
STGKTLGKWE VKNCRSFRAL SICKKVSEPQ EPEEAAPKPD DPCPEGWHTF PSSLSCYKVF
HIERIVRKRN WEEAERFCQA LGAHLPSFSR REEIKDFVHL LKDQFSGQRW LWIGLNKRSP
DLQGSWQWSD RTPVSAVMME PEFQQDFDIR DCAAIKVLDV PWRRVWHLYE DKDYAYWKPF
ACDAKLEWVC QIPKGSTPQM PDWYNPERTG IHGPPVIIEG SEYWFVADPH LNYEEAVLYC
ASNHSFLATI TSFTGLKAIK NKLANISGEE QKWWVKTSEN PIDRYFLGSR RRLWHHFPMT
FGDECLHMSA KTWLVDLSKR ADCNAKLPFI CERYNVSSLE KYSPDPAAKV QCTEKWIPFQ
NKCFLKVNSG PVTFSQASGI CHSYGGTLPS VLSRGEQDFI ISLLPEMEAS LWIGLRWTAY
ERINRWTDNR ELTYSNFHPL LVGRRLSIPT NFFDDESHFH CALILNLKKS PLTGTWNFTS
CSERHSLSLC QKYSETEDGQ PWENTSKTVK YLNNLYKIIS KPLTWHGALK ECMKEKMRLV
SITDPYQQAF LAVQATLRNS SFWIGLSSQD DELNFGWSDG KRLQFSNWAG SNEQLDDCVI
LDTDGFWKTA DCDDNQPGAI CYYPGNETEE EVRALDTAKC PSPVQSTPWI PFQNSCYNFM
ITNNRHKTVT PEEVQSTCEK LHSKAHSLSI RNEEENTFVV EQLLYFNYIA SWVMLGITYE
NNSLMWFDKT ALSYTHWRTG RPTVKNGKFL AGLSTDGFWD IQSFNVIEET LHFYQHSISA
CKIEMVDYED KHNGTLPQFI PYKDGVYSVI QKKVTWYEAL NACSQSGGEL ASVHNPNGKL
FLEDIVNRDG FPLWVGLSSH DGSESSFEWS DGRAFDYVPW QSLQSPGDCV VLYPKGIWRR
EKCLSVKDGA ICYKPTKDKK LIFHVKSSKC PVAKRDGPQW VQYGGHCYAS DQVLHSFSEA
KQVCQELDHS ATVVTIADEN ENKFVSRLMR ENYNITMRVW LGLSQHSLDQ SWSWLDGLDV
TFVKWENKTK DGDGKCSILI ASNETWRKVH CSRGYARAVC KIPLSPDYTG IAILFAVLCL
LGLISLAIWF LLQRSHIRWT GFSSVRYEHG TNEDEVMLPS FHD
