CD19_CALJA
ID CD19_CALJA Reviewed; 558 AA.
AC Q3LRP3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=B-lymphocyte antigen CD19;
DE AltName: Full=Differentiation antigen CD19;
DE AltName: CD_antigen=CD19;
DE Flags: Precursor;
GN Name=CD19;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yamabe E., Kohu K., Suemizu H., Sasaki E., Tanioka Y., Yagita H., Habu S.,
RA Satake M.;
RT "Common marmoset CD19 protein.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as coreceptor for the B-cell antigen receptor
CC complex (BCR) on B-lymphocytes. Decreases the threshold for activation
CC of downstream signaling pathways and for triggering B-cell responses to
CC antigens (By similarity). Activates signaling pathways that lead to the
CC activation of phosphatidylinositol 3-kinase and the mobilization of
CC intracellular Ca(2+) stores. Is not required for early steps during B
CC cell differentiation in the blood marrow. Required for normal
CC differentiation of B-1 cells. Required for normal B cell
CC differentiation and proliferation in response to antigen challenges.
CC Required for normal levels of serum immunoglobulins, and for production
CC of high-affinity antibodies in response to antigen challenge (By
CC similarity). {ECO:0000250|UniProtKB:P15391,
CC ECO:0000250|UniProtKB:P25918}.
CC -!- SUBUNIT: Interacts with CR2/CD21. Part of a complex composed of CD19,
CC CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells.
CC Interacts directly with CD81 (via the second extracellular domain);
CC this interaction is initiated early during biosynthesis in the ER/pre-
CC Golgi compartments and is essential for trafficking and
CC compartmentalization of CD19 receptor on the cell surface of activated
CC B cells. Interacts with VAV. Interacts with GRB2 and SOS when
CC phosphorylated on Tyr-350 and/or Tyr-380. Interacts with PLCG2 when
CC phosphorylated on Tyr-411. Interacts with LYN. Interacts (when tyrosine
CC phosphorylated) with the regulatory p85 subunit of phosphatidylinositol
CC 3-kinase (PIK3R1 or PIK3R2). {ECO:0000250|UniProtKB:P15391}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25918};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25918}.
CC Membrane raft {ECO:0000250|UniProtKB:P25918}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:P25918}.
CC -!- PTM: Phosphorylated on tyrosine following B-cell activation (By
CC similarity). Phosphorylated on tyrosine residues by LYN (By
CC similarity). Tyrosine residues are phosphorylated sequentially after
CC activation of the B cell receptor. Phosphorylation of Tyr-533 is
CC extremely rapid (By similarity). {ECO:0000250|UniProtKB:P15391,
CC ECO:0000250|UniProtKB:P25918}.
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DR EMBL; DQ189219; ABA29630.1; -; mRNA.
DR RefSeq; NP_001254698.1; NM_001267769.1.
DR AlphaFoldDB; Q3LRP3; -.
DR SMR; Q3LRP3; -.
DR STRING; 9483.ENSCJAP00000011318; -.
DR GeneID; 100402637; -.
DR KEGG; cjc:100402637; -.
DR CTD; 930; -.
DR eggNOG; ENOG502STG8; Eukaryota.
DR InParanoid; Q3LRP3; -.
DR OrthoDB; 521520at2759; -.
DR Proteomes; UP000008225; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0019724; P:B cell mediated immunity; ISS:UniProtKB.
DR GO; GO:0002322; P:B cell proliferation involved in immune response; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001923; P:B-1 B cell differentiation; ISS:UniProtKB.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0050864; P:regulation of B cell activation; ISS:UniProtKB.
DR GO; GO:0050855; P:regulation of B cell receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR042341; CD19.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR16674; PTHR16674; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..558
FT /note="B-lymphocyte antigen CD19"
FT /id="PRO_0000244872"
FT TOPO_DOM 21..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..114
FT /note="Ig-like C2-type 1"
FT DOMAIN 177..279
FT /note="Ig-like C2-type 2"
FT REGION 331..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..468
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25918"
FT MOD_RES 350
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT MOD_RES 380
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT MOD_RES 411
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT MOD_RES 441
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT MOD_RES 502
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25918"
FT MOD_RES 533
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25918"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..263
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT DISULFID 98..201
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT DISULFID 135..174
FT /evidence="ECO:0000250|UniProtKB:P15391"
SQ SEQUENCE 558 AA; 61662 MW; 5A8C80EE4F5AADB4 CRC64;
MPPACLLFFL LFLTPMGVRP QEPRLVKVEE GDDAMLLCLE ETSQDPAQQV AWWRESPSLE
PFLKLNLGLP GLGFHVGPWG IWLFIFNVSH QMGGFYLCQP GPPSEKAWQP GWTVSVEGSG
ELFRWNASDL SGQGCGLENR SSEDPSSPSG NLMSSQLYVW AKDRPKIWEG EPPCGLLRDS
LNQTLSQDLT MAPGSTLWLS CGVPPDSVSR GPLSWTHVRP KETNFSLLSL ELKDNRPARD
MWVMEKGLLL PQATAQDAGK YYCHRGNLTI SWHLEITARS ALWHWLVRTG GWKVLAVTLT
YMIFCLGSLV GILHLQRALV LRRKRKRMTD PTRRFFKVTP PPGSGPQNQY GNVLSLPTPT
SGLGRAQRWA AGLGGTAPSY RNPRSDVEAD GTVGSRSPPG AGPEEEEGEG YEEPDSEEGS
EFYENDSSLG QDQLSQDGSG YENPEDEPLG PEDEDSFSNA ESYENEDEEL TQPVSRTMDF
LSPHGSAWDP SREATSLGSQ SYEDMRGILY SAPQLRSIRG QPGPNHEEDA DSYENMDNPD
RPDPPWGGGG HVGTWGAR