LOCUS       NP_038853               1723 aa            linear   ROD 04-AUG-2024
DEFINITION  lymphocyte antigen 75 precursor [Mus musculus].
ACCESSION   NP_038853
VERSION     NP_038853.2
DBSOURCE    REFSEQ: accession NM_013825.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1723)
  AUTHORS   Chen,S.T., Oliveira,T.Y., Gazumyan,A., Cipolla,M. and
            Nussenzweig,M.C.
  TITLE     B cell receptor signaling in germinal centers prolongs survival and
            primes B cells for selection
  JOURNAL   Immunity 56 (3), 547-561 (2023)
   PUBMED   36882061
REFERENCE   2  (residues 1 to 1723)
  AUTHORS   Mlynarczyk,C., Teater,M., Pae,J., Chin,C.R., Wang,L., Arulraj,T.,
            Barisic,D., Papin,A., Hoehn,K.B., Kots,E., Ersching,J.,
            Bandyopadhyay,A., Barin,E., Poh,H.X., Evans,C.M., Chadburn,A.,
            Chen,Z., Shen,H., Isles,H.M., Pelzer,B., Tsialta,I., Doane,A.S.,
            Geng,H., Rehman,M.H., Melnick,J., Morgan,W., Nguyen,D.T.T.,
            Elemento,O., Kharas,M.G., Jaffrey,S.R., Scott,D.W., Khelashvili,G.,
            Meyer-Hermann,M., Victora,G.D. and Melnick,A.
  TITLE     BTG1 mutation yields supercompetitive B cells primed for malignant
            transformation
  JOURNAL   Science 379 (6629), eabj7412 (2023)
   PUBMED   36656933
REFERENCE   3  (residues 1 to 1723)
  AUTHORS   Ford,S.L., O'Sullivan,K.M., Kitching,A.R., Holdsworth,S.R.,
            Gan,P.Y. and Summers,S.A.
  TITLE     Toll-like Receptor 9 Induced Dendritic Cell Activation Promotes
            Anti-Myeloperoxidase Autoimmunity and Glomerulonephritis
  JOURNAL   Int J Mol Sci 24 (2), 1339 (2023)
   PUBMED   36674855
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1723)
  AUTHORS   Jing,Z., McCarron,M.J., Dustin,M.L. and Fooksman,D.R.
  TITLE     Germinal center expansion but not plasmablast differentiation is
            proportional to peptide-MHCII density via CD40-CD40L signaling
            strength
  JOURNAL   Cell Rep 39 (5), 110763 (2022)
   PUBMED   35508132
REFERENCE   5  (residues 1 to 1723)
  AUTHORS   Enterina,J.R., Sarkar,S., Streith,L., Jung,J., Arlian,B.M.,
            Meyer,S.J., Takematsu,H., Xiao,C., Baldwin,T.A., Nitschke,L.,
            Shlomchick,M.J., Paulson,J.C. and Macauley,M.S.
  TITLE     Coordinated changes in glycosylation regulate the germinal center
            through CD22
  JOURNAL   Cell Rep 38 (11), 110512 (2022)
   PUBMED   35294874
REFERENCE   6  (residues 1 to 1723)
  AUTHORS   Guo,M., Gong,S., Maric,S., Misulovin,Z., Pack,M., Mahnke,K.,
            Nussenzweig,M.C. and Steinman,R.M.
  TITLE     A monoclonal antibody to the DEC-205 endocytosis receptor on human
            dendritic cells
  JOURNAL   Hum Immunol 61 (8), 729-738 (2000)
   PUBMED   10980384
REFERENCE   7  (residues 1 to 1723)
  AUTHORS   Kronin,V., Wu,L., Gong,S., Nussenzweig,M.C. and Shortman,K.
  TITLE     DEC-205 as a marker of dendritic cells with regulatory effects on
            CD8 T cell responses
  JOURNAL   Int Immunol 12 (5), 731-735 (2000)
   PUBMED   10784619
REFERENCE   8  (residues 1 to 1723)
  AUTHORS   Guerriero,A., Langmuir,P.B., Spain,L.M. and Scott,E.W.
  TITLE     PU.1 is required for myeloid-derived but not lymphoid-derived
            dendritic cells
  JOURNAL   Blood 95 (3), 879-885 (2000)
   PUBMED   10648399
REFERENCE   9  (residues 1 to 1723)
  AUTHORS   Swiggard,W.J., Mirza,A., Nussenzweig,M.C. and Steinman,R.M.
  TITLE     DEC-205, a 205-kDa protein abundant on mouse dendritic cells and
            thymic epithelium that is detected by the monoclonal antibody
            NLDC-145: purification, characterization, and N-terminal amino acid
            sequence
  JOURNAL   Cell Immunol 165 (2), 302-311 (1995)
   PUBMED   7553896
REFERENCE   10 (residues 1 to 1723)
  AUTHORS   Jiang,W., Swiggard,W.J., Heufler,C., Peng,M., Mirza,A.,
            Steinman,R.M. and Nussenzweig,M.C.
  TITLE     The receptor DEC-205 expressed by dendritic cells and thymic
            epithelial cells is involved in antigen processing
  JOURNAL   Nature 375 (6527), 151-155 (1995)
   PUBMED   7753172
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL935326.13.
            
            On Jun 10, 2007 this sequence version replaced NP_038853.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U19271.1, BC150734.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1723
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 34.54 cM"
     Protein         1..1723
                     /product="lymphocyte antigen 75 precursor"
                     /note="ly-75"
                     /calculated_mol_wt=194520
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2852
     mat_peptide     28..1723
                     /product="Lymphocyte antigen 75. /id=PRO_0000017554"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60767.2)"
                     /calculated_mol_wt=194520
     Region          32..145
                     /region_name="beta-trefoil_Ricin_MRC-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in the macrophage mannose receptor (MRC) family;
                     cl49621"
                     /db_xref="CDD:483961"
     Site            order(48..50,55,57,64..65)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467789"
     Site            order(85..86,96,98,105..106)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467789"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Region          162..209
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(173,175,180,193,200,206,208)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          216..341
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(315,319,321,326,328..331,334..336)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            345
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Region          361..486
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            377
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            order(460,464,465,471,473..476,479..481)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          501..624
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            529
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            order(599,601,608,610..613,616..618)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          643..791
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(750,754,756,776,778..781,784..786)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          821..933
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cd00037"
                     /db_xref="CDD:153057"
     Site            843
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            865
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            order(903,907,909,919..922,925..927)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            934
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O60449; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            935
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Region          952..1091
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(1059,1063,1069,1075,1077..1080,1083..1085)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            1077
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            1104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Region          1122..1223
                     /region_name="Lectin_C"
                     /note="Lectin C-type domain; pfam00059"
                     /db_xref="CDD:459655"
     Site            1226
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Region          1240..1363
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            1321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            1393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Region          1407..1514
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cd00037"
                     /db_xref="CDD:153057"
     Site            order(1487,1491,1493,1497,1499..1502,1506..1508)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          1540..1661
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            1594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            1627
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            order(1634,1637,1639,1645,1647..1650,1653..1655)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            1668..1692
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60767.2)"
     Site            1704
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     Site            1720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60767.2)"
     CDS             1..1723
                     /gene="Ly75"
                     /gene_synonym="CD205; DEC-205; DEC205"
                     /coded_by="NM_013825.4:43..5214"
                     /db_xref="CCDS:CCDS38126.1"
                     /db_xref="GeneID:17076"
                     /db_xref="MGI:MGI:106662"
ORIGIN      
        1 mrtgrvtpgl aagllllllr sfglvepses sgndpftivh entgkciqpl sdwvvaqdcs
       61 gtnnmlwkwv sqhrlfhles qkclglditk atdnlrmfsc dstvmlwwkc ehhslytaaq
      121 yrlalkdgya vantntsdvw kkggseenlc aqpyheiytr dgnsygrpce fpfligetwy
      181 hdcihdedhs gpwcattlsy eydqkwgicl lpesgcegnw ekneqigscy qfnnqeilsw
      241 keayvscqnq gadllsihsa aelayitgke diarlvwlgl nqlysargwe wsdfrplkfl
      301 nwdpgtpvap viggsscarm dtesglwqsv scesqqpyvc kkplnntlel pdvwtytdth
      361 chvgwlpnng fcyllaness swdaahlkck afgadlismh sladvevvvt klhngdvkke
      421 iwtglkntns palfqwsdgt evtltywnen epsvpfnktp ncvsylgklg qwkvqscekk
      481 lryvckkkge itkdaesdkl cppdegwkrh getcykiyek eapfgtncnl titsrfeqef
      541 lnymmknydk slrkyfwtgl rdpdsrgeys wavaqgvkqa vtfsnwnfle paspggcvam
      601 stgktlgkwe vkncrsfral sickkvsepq epeeaapkpd dpcpegwhtf psslscykvf
      661 hierivrkrn weeaerfcqa lgahlpsfsr reeikdfvhl lkdqfsgqrw lwiglnkrsp
      721 dlqgswqwsd rtpvsavmme pefqqdfdir dcaaikvldv pwrrvwhlye dkdyaywkpf
      781 acdaklewvc qipkgstpqm pdwynpertg ihgppviieg seywfvadph lnyeeavlyc
      841 asnhsflati tsftglkaik nklanisgee qkwwvktsen pidryflgsr rrlwhhfpmt
      901 fgdeclhmsa ktwlvdlskr adcnaklpfi cerynvssle kyspdpaakv qctekwipfq
      961 nkcflkvnsg pvtfsqasgi chsyggtlps vlsrgeqdfi isllpemeas lwiglrwtay
     1021 erinrwtdnr eltysnfhpl lvgrrlsipt nffddeshfh calilnlkks pltgtwnfts
     1081 cserhslslc qkysetedgq pwentsktvk ylnnlykiis kpltwhgalk ecmkekmrlv
     1141 sitdpyqqaf lavqatlrns sfwiglssqd delnfgwsdg krlqfsnwag sneqlddcvi
     1201 ldtdgfwkta dcddnqpgai cyypgnetee evraldtakc pspvqstpwi pfqnscynfm
     1261 itnnrhktvt peevqstcek lhskahslsi rneeentfvv eqllyfnyia swvmlgitye
     1321 nnslmwfdkt alsythwrtg rptvkngkfl aglstdgfwd iqsfnvieet lhfyqhsisa
     1381 ckiemvdyed khngtlpqfi pykdgvysvi qkkvtwyeal nacsqsggel asvhnpngkl
     1441 fledivnrdg fplwvglssh dgsessfews dgrafdyvpw qslqspgdcv vlypkgiwrr
     1501 ekclsvkdga icykptkdkk lifhvksskc pvakrdgpqw vqygghcyas dqvlhsfsea
     1561 kqvcqeldhs atvvtiaden enkfvsrlmr enynitmrvw lglsqhsldq swswldgldv
     1621 tfvkwenktk dgdgkcsili asnetwrkvh csrgyaravc kiplspdytg iailfavlcl
     1681 lglislaiwf llqrshirwt gfssvryehg tnedevmlps fhd
//
