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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
 
 
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