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Tyrosine-protein kinase JAK3 (EC 2 7 10 2) (Janus kinase 3) (JAK-3)

 JAK3_MOUSE              Reviewed;        1100 AA.
Q62137; A2RRI3; Q0D2M8; Q61746; Q61747; Q8BTY6; Q8BYU2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-AUG-2007, sequence version 2.
05-DEC-2018, entry version 188.
RecName: Full=Tyrosine-protein kinase JAK3;
EC=2.7.10.2;
AltName: Full=Janus kinase 3;
Short=JAK-3;
Name=Jak3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7518579;
Rane S.G., Reddy E.P.;
"JAK3: a novel JAK kinase associated with terminal differentiation of
hematopoietic cells.";
Oncogene 9:2415-2423(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
MUTAGENESIS OF LEU-853.
STRAIN=BALB/C X 129; TISSUE=Thymus;
PubMed=8605329;
Gurniak C.B., Berg L.J.;
"Murine JAK3 is preferentially expressed in hematopoietic tissues and
lymphocyte precursor cells.";
Blood 87:3151-3160(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
PubMed=8022486; DOI=10.1038/370153a0;
Witthuhn B.A., Silvennoinen O., Miura O., Lai K.S., Cwik C., Liu E.T.,
Ihle J.N.;
"Involvement of the Jak-3 Janus kinase in signalling by interleukins 2
and 4 in lymphoid and myeloid cells.";
Nature 370:153-157(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Heart, Spleen, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISRUPTION PHENOTYPE.
PubMed=7481767; DOI=10.1126/science.270.5237.794;
Thomis D.C., Gurniak C.B., Tivol E., Sharpe A.H., Berg L.J.;
"Defects in B lymphocyte maturation and T lymphocyte activation in
mice lacking Jak3.";
Science 270:794-797(1995).
[7]
DISRUPTION PHENOTYPE.
PubMed=7481769; DOI=10.1126/science.270.5237.800;
Nosaka T., van Deursen J.M., Tripp R.A., Thierfelder W.E.,
Witthuhn B.A., McMickle A.P., Doherty P.C., Grosveld G.C., Ihle J.N.;
"Defective lymphoid development in mice lacking Jak3.";
Science 270:800-802(1995).
[8]
FUNCTION.
PubMed=9016869; DOI=10.1084/jem.185.2.197;
Thomis D.C., Berg L.J.;
"Peripheral expression of Jak3 is required to maintain T lymphocyte
function.";
J. Exp. Med. 185:197-206(1997).
[9]
DISRUPTION PHENOTYPE.
PubMed=9620658;
Baird A.M., Thomis D.C., Berg L.J.;
"T cell development and activation in Jak3-deficient mice.";
J. Leukoc. Biol. 63:669-677(1998).
[10]
INTERACTION WITH MYO18A.
PubMed=10733938; DOI=10.1006/bbrc.2000.2413;
Ji H., Zhai Q., Zhu J., Yan M., Sun L., Liu X., Zheng Z.;
"A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by
IL-2 deprival.";
Biochem. Biophys. Res. Commun. 270:267-271(2000).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Non-receptor tyrosine kinase involved in various
processes such as cell growth, development, or differentiation.
Mediates essential signaling events in both innate and adaptive
immunity and plays a crucial role in hematopoiesis during T-cells
development. In the cytoplasm, plays a pivotal role in signal
transduction via its association with type I receptors sharing the
common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and
IL21R. Following ligand binding to cell surface receptors,
phosphorylates specific tyrosine residues on the cytoplasmic tails
of the receptor, creating docking sites for STATs proteins.
Subsequently, phosphorylates the STATs proteins once they are
recruited to the receptor. Phosphorylated STATs then form
homodimer or heterodimers and translocate to the nucleus to
activate gene transcription. For example, upon IL2R activation by
IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma
chain (IL2RG) subunits inducing the tyrosine phosphorylation of
both receptor subunits on their cytoplasmic domain. Then, STAT5A
AND STAT5B are recruited, phosphorylated and activated by JAK1 and
JAK3. Once activated, dimerized STAT5 translocates to the nucleus
and promotes the transcription of specific target genes in a
cytokine-specific fashion. {ECO:0000269|PubMed:9016869}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- SUBUNIT: Interacts with STAM2 and MYO18A. Interacts with SHB (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Cytoplasm
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q62137-1; Sequence=Displayed;
Name=2;
IsoId=Q62137-2; Sequence=VSP_027575, VSP_027576;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: In contrast with the ubiquitous expression of
the other JAKs, JAK3 is predominantly expressed in hematopoietic
tissues. {ECO:0000269|PubMed:8605329}.
-!- DOMAIN: Possesses two phosphotransferase domains. The second one
contains the catalytic domain, while the presence of a
pseudokinase domain is required for suppression of basal activity
of JAK3.
-!- PTM: Autophosphorylated, leading to regulate its activity. IL2
promotes phosphorylation on tyrosine residues, including
autophosphorylation on Tyr-781 (By similarity). Dephosphorylation
of Tyr-976 and Tyr-977 by PTPN2 negatively regulates cytokine-
mediated signaling (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show a severe block in B-cell
development at the pre-B stage in the bone marrow. Additionally,
they possesses small thymuses revealing a defect in T-cell
development. The distribution of developmental subsets is
relatively normal, suggesting a block in the expansion of early T-
cell progenitors. Peripheral T-cells are present at normal or
increased numbers but are functionally incompetent.
{ECO:0000269|PubMed:7481767, ECO:0000269|PubMed:7481769,
ECO:0000269|PubMed:9620658}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. JAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA21415.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAA21565.1; Type=Frameshift; Positions=222, 232; Evidence={ECO:0000305};
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EMBL; L33768; AAA21415.1; ALT_FRAME; mRNA.
EMBL; L40172; AAC42085.1; -; mRNA.
EMBL; L32955; AAA21565.1; ALT_FRAME; mRNA.
EMBL; AK038268; BAC29956.1; -; mRNA.
EMBL; AK142178; BAE24964.1; -; mRNA.
EMBL; AK156646; BAE33790.1; -; mRNA.
EMBL; AK164520; BAE37819.1; -; mRNA.
EMBL; AK088365; BAC40305.1; -; mRNA.
EMBL; BC105577; AAI05578.1; -; mRNA.
EMBL; BC131646; AAI31647.1; -; mRNA.
EMBL; BC131647; AAI31648.1; -; mRNA.
CCDS; CCDS22403.1; -. [Q62137-1]
PIR; I58401; I58401.
PIR; S48053; S48053.
RefSeq; NP_001177759.1; NM_001190830.1.
RefSeq; NP_034719.2; NM_010589.6.
UniGene; Mm.249645; -.
UniGene; Mm.476857; -.
ProteinModelPortal; Q62137; -.
SMR; Q62137; -.
BioGrid; 200858; 5.
IntAct; Q62137; 2.
MINT; Q62137; -.
STRING; 10090.ENSMUSP00000060073; -.
BindingDB; Q62137; -.
ChEMBL; CHEMBL5250; -.
iPTMnet; Q62137; -.
PhosphoSitePlus; Q62137; -.
EPD; Q62137; -.
PaxDb; Q62137; -.
PRIDE; Q62137; -.
GeneID; 16453; -.
KEGG; mmu:16453; -.
UCSC; uc009mel.2; mouse. [Q62137-1]
CTD; 3718; -.
MGI; MGI:99928; Jak3.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
HOVERGEN; HBG006195; -.
InParanoid; Q62137; -.
KO; K11218; -.
PhylomeDB; Q62137; -.
TreeFam; TF327041; -.
BRENDA; 2.7.10.2; 3474.
PRO; PR:Q62137; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_JAK3; -.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IMP:BHF-UCL.
GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; IDA:MGI.
GO; GO:0030218; P:erythrocyte differentiation; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0035771; P:interleukin-4-mediated signaling pathway; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0048535; P:lymph node development; TAS:MGI.
GO; GO:0002731; P:negative regulation of dendritic cell cytokine production; IMP:BHF-UCL.
GO; GO:0045221; P:negative regulation of FasL biosynthetic process; IMP:BHF-UCL.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:BHF-UCL.
GO; GO:0032695; P:negative regulation of interleukin-12 production; IMP:BHF-UCL.
GO; GO:0050868; P:negative regulation of T cell activation; IMP:BHF-UCL.
GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; IMP:BHF-UCL.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IMP:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:BHF-UCL.
GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IMP:BHF-UCL.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0070232; P:regulation of T cell apoptotic process; IMP:BHF-UCL.
GO; GO:0070672; P:response to interleukin-15; TAS:BHF-UCL.
GO; GO:0070669; P:response to interleukin-2; TAS:BHF-UCL.
GO; GO:0070670; P:response to interleukin-4; ISS:BHF-UCL.
GO; GO:0071104; P:response to interleukin-9; TAS:BHF-UCL.
GO; GO:0043029; P:T cell homeostasis; IMP:BHF-UCL.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IBA:GO_Central.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR000299; FERM_domain.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
InterPro; IPR020775; Tyr_kinase_non-rcpt_Jak3.
Pfam; PF07714; Pkinase_Tyr; 2.
PIRSF; PIRSF000636; TyrPK_Jak; 1.
PRINTS; PR01823; JANUSKINASE.
PRINTS; PR01826; JANUSKINASE3.
PRINTS; PR00109; TYRKINASE.
SMART; SM00295; B41; 1.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 2.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Immunity; Innate immunity; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat; SH2 domain; Transferase; Tyrosine-protein kinase.
CHAIN 1 1100 Tyrosine-protein kinase JAK3.
/FTId=PRO_0000088116.
DOMAIN 24 353 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 372 472 SH2; atypical.
DOMAIN 517 777 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 818 1100 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 824 832 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 223 Interaction with
cytokine/interferon/growth hormone
receptors. {ECO:0000250}.
ACT_SITE 945 945 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 851 851 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 781 781 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P52333}.
MOD_RES 900 900 Phosphotyrosine.
{ECO:0000250|UniProtKB:P52333}.
MOD_RES 935 935 Phosphotyrosine.
{ECO:0000250|UniProtKB:P52333}.
MOD_RES 976 976 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P52333}.
MOD_RES 977 977 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P52333}.
VAR_SEQ 284 284 E -> EVLGLGLRSGVRGEAWRLVKKPVRTIRKVASPGRAD
CTTGQGGGVNLKVGPGMELPQGLTWGVTRRVRLDRGRGRTE
GDSMDWISGHDPTRPVFSPLTSSPPPHKWRWEGGRRGGCAG
SRSVIPWLLSLFLFFFFNGFARQGFSYSSGCPGTHFVRPGW
PRTQKSACLCLSSAVIKGRVPLRRYCLSFLPQ (in
isoform 2). {ECO:0000303|PubMed:7518579}.
/FTId=VSP_027575.
VAR_SEQ 379 379 L -> LGASWGQQWGWGWAARTVLGWTWLLSWPRL (in
isoform 2). {ECO:0000303|PubMed:7518579}.
/FTId=VSP_027576.
MUTAGEN 853 853 L->R: Loss of activity.
{ECO:0000269|PubMed:8605329}.
CONFLICT 62 62 G -> A (in Ref. 1; AAA21415 and 2;
AAA21565). {ECO:0000305}.
CONFLICT 277 277 S -> P (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 281 283 GDQ -> ND (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 301 301 K -> N (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 362 362 P -> A (in Ref. 1; AAA21415).
{ECO:0000305}.
CONFLICT 371 372 EL -> DV (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 390 390 G -> A (in Ref. 1; AAA21415).
{ECO:0000305}.
CONFLICT 454 454 Missing (in Ref. 4; BAC40305).
{ECO:0000305}.
CONFLICT 467 467 N -> Y (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 490 490 T -> N (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 518 519 EW -> G (in Ref. 1; AAA21415).
{ECO:0000305}.
CONFLICT 535 535 R -> S (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 699 699 C -> G (in Ref. 4; BAC40305/BAC29956/
BAE24964/BAE33790/BAE37819).
{ECO:0000305}.
CONFLICT 716 717 SG -> QR (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 800 800 G -> VA (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 826 826 K -> N (in Ref. 5; AAI31647).
{ECO:0000305}.
CONFLICT 841 841 Missing (in Ref. 1; AAA21415).
{ECO:0000305}.
CONFLICT 857 857 G -> V (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 909 909 F -> L (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 915 916 AR -> G (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 916 916 R -> A (in Ref. 1; AAA21415).
{ECO:0000305}.
CONFLICT 1032 1032 R -> S (in Ref. 4; BAC40305/BAC29956/
BAE24964/BAE33790/BAE37819).
{ECO:0000305}.
CONFLICT 1074 1074 W -> V (in Ref. 1; AAA21415).
{ECO:0000305}.
CONFLICT 1077 1077 S -> E (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 1085 1085 G -> A (in Ref. 2; AAA21565).
{ECO:0000305}.
CONFLICT 1093 1093 A -> G (in Ref. 1; AAA21415).
{ECO:0000305}.
CONFLICT 1093 1093 A -> P (in Ref. 2; AAA21565).
{ECO:0000305}.
SEQUENCE 1100 AA; 122641 MW; 979A120861ED37C1 CRC64;
MAPPSEETPL IPQRSCSLSS SEAGALHVLL PPRGPGPPQR LSFSFGDYLA EDLCVRAAKA
CGILPVYHSL FALATEDFSC WFPPSHIFCI EDVDTQVLVY RLRFYFPDWF GLETCHRFGL
RKDLTSAILD LHVLEHLFAQ HRSDLVSGRL PVGLSMKEQG EFLSLAVLDL AQMAREQAQR
PGELLKTVSY KACLPPSLRD VIQGQNFVTR RRIRRTVVLA LRRVVACQAD RYALMAKYIL
DLERLHPAAT TETFRVGLPG AQEEPGLLRV AGDNGISWSS GDQELFQTFC DFPEIVDVSI
KQAPRVGPAG EHRLVTVTRM DGHILEAEFP GLPEALSFVA LVDGYFRLIC DSRHYFCKEV
APPRLLEEEA ELCHGPITLD FAIHKLKAAG SLPGTYILRR SPQDYDSFLL TACVQTPLGP
DYKGCLIRQD PSGAFSLVGL SQPHRSLREL LAACWNSGLR VDGAALNLTS CCAPRPKEKS
NLIVVRRGCT PAPAPGCSPS CCALTQLSFH TIPTDSLEWH ENLGHGSFTK IFRGRRREVV
DGETHDSEVL LKVMDSRHRN CMESFLEAAS LMSQVSYPHL VLLHGVCMAG DSIMVQEFVY
LGAIDMYLRK RGHLVSASWK LQVTKQLAYA LNYLEDKGLP HGNVSARKVL LAREGGDGNP
PFIKLSDPGV SPTVLSLEML TDRIPWVAPE CLQEAQTLCL EADKWGFGAT TWEVFSGGPA
HITSLEPAKK LKFYEDQGQL PALKWTELAG LITQCMAYDP GRRPSFRAIL RDLNGLITSD
YELLSDPTPG IPSPRDELCG GAQLYACQDP AIFEERHLKY ISLLGKGNFG SVELCRYDPL
GDNTGPLVAV KQLQHSGPDQ QRDFQREIQI LKALHSDFIV KYRGVSYGPG RQSLRLVMEY
LPSGCLRDFL QRHRARLHTD RLLLFAWQIC KGMEYLGARR CVHRDLAARN ILVESEAHVK
IADFGLAKLL PLGKDYYVVR EPGQSPIFWY APESLSDNIF SRQSDVWSFG VVLYELFTYC
DKSCSPSAEF LRMMGPEREG PPLCRLLELL AEGRRLPPPP TCPTEVQELM QLCWAPSPHD
RPAFGTLSPQ LDALWRGRPG


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