CD19_MOUSE
ID CD19_MOUSE Reviewed; 547 AA.
AC P25918; Q542B2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 180.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=1714482;
RA Zhou L.J., Ord D.C., Hughes A.L., Tedder T.F.;
RT "Structure and domain organization of the CD19 antigen of human, mouse, and
RT guinea pig B lymphocytes. Conservation of the extensive cytoplasmic
RT domain.";
RL J. Immunol. 147:1424-1432(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Spleen;
RX PubMed=1370948; DOI=10.1007/bf00189519;
RA Zhou L.J., Ord D.C., Omori S.A., Tedder T.F.;
RT "Structure of the genes encoding the CD19 antigen of human and mouse B
RT lymphocytes.";
RL Immunogenetics 35:102-111(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-547.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=2472450;
RA Tedder T.F., Isaacs C.M.;
RT "Isolation of cDNAs encoding the CD19 antigen of human and mouse B
RT lymphocytes. A new member of the immunoglobulin superfamily.";
RL J. Immunol. 143:712-717(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=1375324; DOI=10.1128/mcb.12.6.2662-2672.1992;
RA Kozmik Z., Wang S., Doerfler P., Adams B., Busslinger M.;
RT "The promoter of the CD19 gene is a target for the B-cell-specific
RT transcription factor BSAP.";
RL Mol. Cell. Biol. 12:2662-2672(1992).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=7542548; DOI=10.1016/1074-7613(95)90157-4;
RA Engel P., Zhou L.J., Ord D.C., Sato S., Koller B., Tedder T.F.;
RT "Abnormal B lymphocyte development, activation, and differentiation in mice
RT that lack or overexpress the CD19 signal transduction molecule.";
RL Immunity 3:39-50(1995).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=7543183; DOI=10.1038/376352a0;
RA Rickert R.C., Rajewsky K., Roes J.;
RT "Impairment of T-cell-dependent B-cell responses and B-1 cell development
RT in CD19-deficient mice.";
RL Nature 376:352-355(1995).
RN [9]
RP FUNCTION.
RX PubMed=9382888; DOI=10.1084/jem.186.11.1897;
RA Buhl A.M., Pleiman C.M., Rickert R.C., Cambier J.C.;
RT "Qualitative regulation of B cell antigen receptor signaling by CD19:
RT selective requirement for PI3-kinase activation, inositol-1,4,5-
RT trisphosphate production and Ca2+ mobilization.";
RL J. Exp. Med. 186:1897-1910(1997).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9317126;
RA Sato S., Miller A.S., Howard M.C., Tedder T.F.;
RT "Regulation of B lymphocyte development and activation by the
RT CD19/CD21/CD81/Leu 13 complex requires the cytoplasmic domain of CD19.";
RL J. Immunol. 159:3278-3287(1997).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12387743; DOI=10.1016/s1074-7613(02)00426-0;
RA Wang Y., Brooks S.R., Li X., Anzelon A.N., Rickert R.C., Carter R.H.;
RT "The physiologic role of CD19 cytoplasmic tyrosines.";
RL Immunity 17:501-514(2002).
RN [12]
RP PHOSPHORYLATION AT SER-225.
RX PubMed=15378723; DOI=10.1002/rcm.1604;
RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT purification and linear ion trap mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-402; TYR-493 AND
RP TYR-522, AND TISSUE SPECIFICITY.
RX PubMed=20101619; DOI=10.1002/eji.200939848;
RA Ishiura N., Nakashima H., Watanabe R., Kuwano Y., Adachi T., Takahashi Y.,
RA Tsubata T., Okochi H., Tamaki K., Tedder T.F., Fujimoto M.;
RT "Differential phosphorylation of functional tyrosines in CD19 modulates B-
RT lymphocyte activation.";
RL Eur. J. Immunol. 40:1192-1204(2010).
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 (PubMed:9382888, PubMed:12387743,
CC PubMed:20101619). Is not required for early steps during B cell
CC differentiation in the blood marrow (PubMed:7542548, PubMed:7543183,
CC PubMed:9317126). Required for normal differentiation of B-1 cells
CC (PubMed:7542548, PubMed:7543183, PubMed:12387743). Required for normal
CC B cell differentiation and proliferation in response to antigen
CC challenges (PubMed:7542548, PubMed:9317126, PubMed:12387743). Required
CC for normal levels of serum immunoglobulins, and for production of high-
CC affinity antibodies in response to antigen challenge (PubMed:7542548,
CC PubMed:7543183, PubMed:12387743). {ECO:0000250|UniProtKB:P15391,
CC ECO:0000269|PubMed:12387743, ECO:0000269|PubMed:20101619,
CC ECO:0000269|PubMed:7542548, ECO:0000269|PubMed:7543183,
CC ECO:0000269|PubMed:9317126, ECO:0000269|PubMed:9382888}.
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 when
CC phosphorylated on Tyr-346 and/or Tyr-376. Interacts with PLCG2 when
CC phosphorylated on Tyr-402. 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:0000269|PubMed:12387743,
CC ECO:0000269|PubMed:20101619, ECO:0000269|PubMed:7543183}; Single-pass
CC type I membrane protein {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:20101619}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected on B cells in spleen, bone marrow, thymus
CC and lymph nodes (PubMed:12387743, PubMed:7542548, PubMed:20101619).
CC Detected on peripheral blood lymphocytes (at protein level)
CC (PubMed:7543183). {ECO:0000269|PubMed:12387743,
CC ECO:0000269|PubMed:20101619, ECO:0000269|PubMed:7542548,
CC ECO:0000269|PubMed:7543183}.
CC -!- PTM: Phosphorylated on tyrosine following B-cell activation
CC (PubMed:20101619). 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-522 is
CC extremely rapid, followed by phosphorylation at Tyr-402. In contrast,
CC phosphorylation of Tyr-493 appears more slowly and is more transient,
CC returning rapidly to basal levels (PubMed:20101619).
CC {ECO:0000250|UniProtKB:P15391, ECO:0000269|PubMed:20101619}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC ratio, thrive and are fertile (PubMed:7542548). Mutant mice display
CC normal differentiation and expansion of pro-B cells, pre-B cells,
CC immature B cells and resting mature B cells in bone marrow
CC (PubMed:7542548, PubMed:7543183, PubMed:9317126). Number and surface
CC phenotype of conventional B cells in spleen, Peyer's patch and lymph
CC nodes appear normal (PubMed:7543183). In contrast, the numbers of B-1
CC cells are decreased to 10-20% of the normal values in the peritoneal
CC cavity, together with a severe reduction of serum IgM levels
CC (PubMed:7542548, PubMed:7543183, PubMed:12387743). Likewise, mutant
CC mice display severely reduced serum IgG1 and IgE levels
CC (PubMed:7543183). Mutant mice display severely reduced B cell responses
CC to antigens, with a strong decrease in the production of serum
CC antibodies after an antigenic challenge, and defective production of
CC high-affinity antibodies (PubMed:7543183).
CC {ECO:0000269|PubMed:12387743, ECO:0000269|PubMed:7542548,
CC ECO:0000269|PubMed:7543183, ECO:0000269|PubMed:9317126}.
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DR EMBL; M62542; AAA37388.1; -; Genomic_DNA.
DR EMBL; M62553; AAA37390.1; -; Genomic_DNA.
DR EMBL; M62551; AAA37390.1; JOINED; Genomic_DNA.
DR EMBL; M62552; AAA37390.1; JOINED; Genomic_DNA.
DR EMBL; AK089835; BAC40973.1; -; mRNA.
DR EMBL; CH466531; EDL17351.1; -; Genomic_DNA.
DR EMBL; M28240; AAA74753.1; -; Genomic_DNA.
DR EMBL; M84372; AAA37389.1; -; Genomic_DNA.
DR CCDS; CCDS21828.1; -.
DR PIR; B45808; B45808.
DR RefSeq; NP_033974.2; NM_009844.2.
DR RefSeq; XP_006507346.1; XM_006507283.2.
DR AlphaFoldDB; P25918; -.
DR SMR; P25918; -.
DR BioGRID; 198576; 1.
DR IntAct; P25918; 3.
DR STRING; 10090.ENSMUSP00000032968; -.
DR GlyGen; P25918; 7 sites.
DR iPTMnet; P25918; -.
DR PhosphoSitePlus; P25918; -.
DR PaxDb; P25918; -.
DR PeptideAtlas; P25918; -.
DR PRIDE; P25918; -.
DR ProteomicsDB; 281513; -.
DR ABCD; P25918; 8 sequenced antibodies.
DR Antibodypedia; 4237; 4853 antibodies from 55 providers.
DR DNASU; 12478; -.
DR Ensembl; ENSMUST00000206325; ENSMUSP00000145803; ENSMUSG00000030724.
DR GeneID; 12478; -.
DR KEGG; mmu:12478; -.
DR UCSC; uc009jrb.1; mouse.
DR CTD; 930; -.
DR MGI; MGI:88319; Cd19.
DR VEuPathDB; HostDB:ENSMUSG00000030724; -.
DR eggNOG; ENOG502STG8; Eukaryota.
DR GeneTree; ENSGT00390000014991; -.
DR HOGENOM; CLU_038774_0_0_1; -.
DR InParanoid; P25918; -.
DR OMA; LWLPCGV; -.
DR OrthoDB; 521520at2759; -.
DR TreeFam; TF338293; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 12478; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cd19; mouse.
DR PRO; PR:P25918; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P25918; protein.
DR Bgee; ENSMUSG00000030724; Expressed in peripheral lymph node and 43 other tissues.
DR ExpressionAtlas; P25918; baseline and differential.
DR Genevisible; P25918; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0019724; P:B cell mediated immunity; IMP: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; IDA:MGI.
DR GO; GO:0001923; P:B-1 B cell differentiation; IMP:UniProtKB.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP: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; IMP: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 1: Evidence at protein 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..16
FT PROPEP 17..18
FT /evidence="ECO:0000255"
FT /id="PRO_0000014649"
FT CHAIN 19..547
FT /note="B-lymphocyte antigen CD19"
FT /id="PRO_0000014650"
FT TOPO_DOM 19..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 171..271
FT /note="Ig-like C2-type 2"
FT REGION 330..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15378723"
FT MOD_RES 346
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT MOD_RES 376
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT MOD_RES 402
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20101619"
FT MOD_RES 432
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT MOD_RES 493
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20101619,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20101619"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..259
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT DISULFID 97..197
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT DISULFID 134..169
FT /evidence="ECO:0000250|UniProtKB:P15391"
FT CONFLICT 207
FT /note="G -> A (in Ref. 2; AAA37390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 60149 MW; DDC34A3E23410C8D CRC64;
MPSPLPVSFL LFLTLVGGRP QKSLLVEVEE GGNVVLPCLP DSSPVSSEKL AWYRGNQSTP
FLELSPGSPG LGLHVGSLGI LLVIVNVSDH MGGFYLCQKR PPFKDIWQPA WTVNVEDSGE
MFRWNASDVR DLDCDLRNRS SGSHRSTSGS QLYVWAKDHP KVWGTKPVCA PRGSSLNQSL
INQDLTVAPG STLWLSCGVP PVPVAKGSIS WTHVHPRRPN VSLLSLSLGG EHPVREMWVW
GSLLLLPQAT ALDEGTYYCL RGNLTIERHV KVIARSAVWL WLLRTGGWIV PVVTLVYVIF
CMVSLVAFLY CQRAFILRRK RKRMTDPARR FFKVTPPSGN GTQNQYGNVL SLPTSTSGQA
HAQRWAAGLG SVPGSYGNPR IQVQDTGAQS HETGLEEEGE AYEEPDSEEG SEFYENDSNL
GQDQVSQDGS GYENPEDEPM GPEEEDSFSN AESYENADEE LAQPVGRMMD FLSPHGSAWD
PSREASSLGS QSYEDMRGIL YAAPQLHSIQ SGPSHEEDAD SYENMDKSDD LEPAWEGEGH
MGTWGTT
