ID   CD20_CANLF              Reviewed;         297 AA.
AC   Q3C2E2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=B-lymphocyte antigen CD20;
DE   AltName: Full=Membrane-spanning 4-domains subfamily A member 1;
DE   AltName: CD_antigen=CD20;
GN   Name=MS4A1; Synonyms=CD20;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16061290; DOI=10.1016/j.vetimm.2005.05.011;
RA   Kano R., Inoue C., Okano H., Yamazaki J., Takahashi T., Watari T.,
RA   Tokuriki M., Hasegawa A.;
RT   "Canine CD20 gene.";
RL   Vet. Immunol. Immunopathol. 108:265-268(2005).
CC   -!- FUNCTION: B-lymphocyte-specific membrane protein that plays a role in
CC       the regulation of cellular calcium influx necessary for the
CC       development, differentiation, and activation of B-lymphocytes.
CC       Functions as a store-operated calcium (SOC) channel component promoting
CC       calcium influx after activation by the B-cell receptor/BCR.
CC       {ECO:0000250|UniProtKB:P11836}.
CC   -!- SUBUNIT: Forms homotetramers. Interacts with the heavy and light chains
CC       of cell surface IgM, the antigen-binding components of the BCR.
CC       {ECO:0000250|UniProtKB:P11836}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11836};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P11836}. Cell
CC       membrane {ECO:0000250|UniProtKB:P11836}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P11836}. Note=Constitutively associated with
CC       membrane rafts. {ECO:0000250|UniProtKB:P11836}.
CC   -!- TISSUE SPECIFICITY: Expressed in PBMCs and lymph node from healthy
CC       dogs, in B-cells of canine lymphoma, but not in T-cell lymphoma cells
CC       and non-T and non-B-cell lymphoma cells. {ECO:0000269|PubMed:16061290}.
CC   -!- PTM: Phosphorylated. Might be functionally regulated by protein
CC       kinase(s) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MS4A family. {ECO:0000305}.
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DR   EMBL; AB210085; BAE47068.1; -; mRNA.
DR   RefSeq; NP_001041493.1; NM_001048028.1.
DR   AlphaFoldDB; Q3C2E2; -.
DR   SMR; Q3C2E2; -.
DR   STRING; 9612.ENSCAFP00000035044; -.
DR   PaxDb; Q3C2E2; -.
DR   PRIDE; Q3C2E2; -.
DR   ABCD; Q3C2E2; 1 sequenced antibody.
DR   GeneID; 485430; -.
DR   KEGG; cfa:485430; -.
DR   CTD; 931; -.
DR   eggNOG; ENOG502S6Z3; Eukaryota.
DR   InParanoid; Q3C2E2; -.
DR   OrthoDB; 1251311at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR   InterPro; IPR007237; CD20-like.
DR   InterPro; IPR030417; MS4A.
DR   InterPro; IPR030418; MS4A1.
DR   PANTHER; PTHR23320; PTHR23320; 1.
DR   PANTHER; PTHR23320:SF79; PTHR23320:SF79; 1.
DR   Pfam; PF04103; CD20; 1.
PE   2: Evidence at transcript level;
KW   B-cell activation; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..297
FT                   /note="B-lymphocyte antigen CD20"
FT                   /id="PRO_0000158626"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          274..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19437"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19437"
FT   LIPID           220
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   297 AA;  33056 MW;  B48B3CF88301F249 CRC64;
     MTTPRNSMSG TLPVDPMKSP TAMYPVQKII PKRMPSVVGP TQNFFMRESK TLGAVQIMNG
     LFHIALGSLL MIHTDVCAPI CITMWYPLWG GIMFIISGSL LAAADKNPRK SLVKGKMIMN
     SLSLFAAISG IIFLIMDIFN ITISHFFKME NLNLIKAPMP YVDIHNCDPA NPSEKNSLSI
     QYCGSIRSVF LGVFAVMLIF AFFQKLVTAG IVENEWKKLC SKPKSDVVVL LAAEEKKEQP
     IETTEEMVEL TEIASQPKKE EDIEIIPVQE EEGELEINFA EPPQEQESSP IENDSIP