LOCUS       NP_068693                290 aa            linear   ROD 12-JUN-2025
DEFINITION  programmed cell death 1 ligand 1 precursor [Mus musculus].
ACCESSION   NP_068693
VERSION     NP_068693.1
DBSOURCE    REFSEQ: accession NM_021893.3
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 290)
  AUTHORS   Wu,Z., Shan,Q., Jiang,Y., Huang,W., Wang,Z., Zhuang,Y., Liu,J.,
            Li,T., Yang,Z., Li,C., Wei,T., Wen,C., Cui,W., Qiu,Z., Liu,X. and
            Wang,Z.
  TITLE     Irreversible electroporation combined with PD-L1/IL-6 dual blockade
            promotes anti-tumor immunity via cDC2/CD4+T cell axis in MHC-I
            deficient pancreatic cancer
  JOURNAL   Cancer Lett 617, 217620 (2025)
   PUBMED   40068706
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Borys,S.M., Reilly,S.P., Magill,I., Zemmour,D. and Brossay,L.
  TITLE     NK cells restrain cytotoxic CD8+ T cells in the submandibular gland
            via PD-1-PD-L1
  JOURNAL   Sci Immunol 9 (102), eadl2967 (2024)
   PUBMED   39705335
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Lazar-Molnar,E., Yan,Q., Cao,E., Ramagopal,U., Nathenson,S.G. and
            Almo,S.C.
  TITLE     Crystal structure of the complex between programmed death-1 (PD-1)
            and its ligand PD-L2
  JOURNAL   Proc Natl Acad Sci U S A 105 (30), 10483-10488 (2008)
   PUBMED   18641123
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Habicht,A., Dada,S., Jurewicz,M., Fife,B.T., Yagita,H., Azuma,M.,
            Sayegh,M.H. and Guleria,I.
  TITLE     A link between PDL1 and T regulatory cells in fetomaternal
            tolerance
  JOURNAL   J Immunol 179 (8), 5211-5219 (2007)
   PUBMED   17911606
  REMARK    GeneRIF: Interactions between PD-L1 and T regulatory cells regulate
            the maternal alloimmune response against paternal antigens on the
            fetus.
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Carter,L.L., Leach,M.W., Azoitei,M.L., Cui,J., Pelker,J.W.,
            Jussif,J., Benoit,S., Ireland,G., Luxenberg,D., Askew,G.R.,
            Milarski,K.L., Groves,C., Brown,T., Carito,B.A., Percival,K.,
            Carreno,B.M., Collins,M. and Marusic,S.
  TITLE     PD-1/PD-L1, but not PD-1/PD-L2, interactions regulate the severity
            of experimental autoimmune encephalomyelitis
  JOURNAL   J Neuroimmunol 182 (1-2), 124-134 (2007)
   PUBMED   17182110
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Guleria,I., Khosroshahi,A., Ansari,M.J., Habicht,A., Azuma,M.,
            Yagita,H., Noelle,R.J., Coyle,A., Mellor,A.L., Khoury,S.J. and
            Sayegh,M.H.
  TITLE     A critical role for the programmed death ligand 1 in fetomaternal
            tolerance
  JOURNAL   J Exp Med 202 (2), 231-237 (2005)
   PUBMED   16027236
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Dong,H., Zhu,G., Tamada,K., Flies,D.B., van Deursen,J.M. and
            Chen,L.
  TITLE     B7-H1 determines accumulation and deletion of intrahepatic CD8(+) T
            lymphocytes
  JOURNAL   Immunity 20 (3), 327-336 (2004)
   PUBMED   15030776
  REMARK    GeneRIF: B7-H1 regulates the accumulation and deletion of
            intrahepatic CD8(+) T cells which resulted in accelerated liver
            damage in experimental autoimmune hepatitis.
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Tamura,H., Dong,H., Zhu,G., Sica,G.L., Flies,D.B., Tamada,K. and
            Chen,L.
  TITLE     B7-H1 costimulation preferentially enhances CD28-independent
            T-helper cell function
  JOURNAL   Blood 97 (6), 1809-1816 (2001)
   PUBMED   11238124
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Latchman,Y., Wood,C.R., Chernova,T., Chaudhary,D., Borde,M.,
            Chernova,I., Iwai,Y., Long,A.J., Brown,J.A., Nunes,R.,
            Greenfield,E.A., Bourque,K., Boussiotis,V.A., Carter,L.L.,
            Carreno,B.M., Malenkovich,N., Nishimura,H., Okazaki,T., Honjo,T.,
            Sharpe,A.H. and Freeman,G.J.
  TITLE     PD-L2 is a second ligand for PD-1 and inhibits T cell activation
  JOURNAL   Nat Immunol 2 (3), 261-268 (2001)
   PUBMED   11224527
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Freeman,G.J., Long,A.J., Iwai,Y., Bourque,K., Chernova,T.,
            Nishimura,H., Fitz,L.J., Malenkovich,N., Okazaki,T., Byrne,M.C.,
            Horton,H.F., Fouser,L., Carter,L., Ling,V., Bowman,M.R.,
            Carreno,B.M., Collins,M., Wood,C.R. and Honjo,T.
  TITLE     Engagement of the PD-1 immunoinhibitory receptor by a novel B7
            family member leads to negative regulation of lymphocyte activation
  JOURNAL   J Exp Med 192 (7), 1027-1034 (2000)
   PUBMED   11015443
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC119228.10, BY193530.1,
            AF317088.1 and AI645624.1.
            
            Summary: The protein encoded by this gene is an immune inhibitory
            receptor ligand that is expressed by hematopoietic and
            non-hematopoietic cells, such as T cells and B cells and various
            types of tumor cells. The encoded protein is a type I transmembrane
            protein that has immunoglobulin V-like and C-like domains.
            Interaction of this ligand with its receptor inhibits T-cell
            activation and cytokine production. During infection or
            inflammation of normal tissue, this interaction is important for
            preventing autoimmunity by maintaining homeostasis of the immune
            response. In tumor microenvironments, this interaction provides an
            immune escape for tumor cells through cytotoxic T-cell
            inactivation. Mice deficient for this gene display a variety of
            phenotypes including decreased allogeneic fetal survival rates and
            severe experimental autoimmune encephalomyelitis. [provided by
            RefSeq, Sep 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            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 :: BC066841.1, AK154403.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 23.88 cM"
     Protein         1..290
                     /product="programmed cell death 1 ligand 1 precursor"
                     /note="programmed cell death 1 ligand 1; B7 homolog 1;
                     PDCD1 ligand 1"
                     /calculated_mol_wt=30762
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2037
     mat_peptide     19..290
                     /product="Programmed cell death 1 ligand 1.
                     /id=PRO_0000014554"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP73.1)"
                     /calculated_mol_wt=30762
     Region          21..130
                     /region_name="IgV_PDl1"
                     /note="Immunoglobulin Variable (IgV) domain of Programmed
                     death ligand 1 (PD-L1); cd20947"
                     /db_xref="CDD:409539"
     Region          21..41
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409539"
     Region          21..24
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409539"
     Region          26..31
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409539"
     Region          33..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409539"
     Site            35
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP73.1)"
     Region          42..53
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409539"
     Region          53..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409539"
     Region          54..62
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409539"
     Region          63..74
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409539"
     Region          63..68
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409539"
     Region          70..74
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409539"
     Region          75..116
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409539"
     Region          84..88
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409539"
     Region          96..103
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409539"
     Region          107..117
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409539"
     Region          117..121
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409539"
     Region          121..130
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409539"
     Region          122..130
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409539"
     Region          138..223
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          150..154
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          163..167
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP73.1)"
     Region          194..198
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            199
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP73.1)"
     Region          205..210
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP73.1)"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP73.1)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP73.1)"
     CDS             1..290
                     /gene="Cd274"
                     /gene_synonym="A530045L16Rik; B7h1; Pdcd1l1; Pdcd1lg1;
                     Pdl1"
                     /coded_by="NM_021893.3:84..956"
                     /db_xref="CCDS:CCDS29735.1"
                     /db_xref="GeneID:60533"
                     /db_xref="MGI:MGI:1926446"
ORIGIN      
        1 mrifagiift acchllraft itapkdlyvv eygsnvtmec rfpvereldl lalvvyweke
       61 deqviqfvag eedlkpqhsn frgraslpkd qllkgnaalq itdvklqdag vycciisygg
      121 adykritlkv napyrkinqr isvdpatseh elicqaegyp eaeviwtnsd hqpvsgkrsv
      181 ttsrtegmll nvtsslrvna tandvfyctf wrsqpgqnht aeliipelpa thppqnrthw
      241 vllgsillfl ivvstvllfl rkqvrmldve kcgvedtssk nrndtqfeet
//
