PAK4_MOUSE
ID PAK4_MOUSE Reviewed; 593 AA.
AC Q8BTW9; Q6ZPX0; Q80Z97; Q9CS71;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Serine/threonine-protein kinase PAK 4;
DE EC=2.7.11.1;
DE AltName: Full=p21-activated kinase 4;
DE Short=PAK-4;
GN Name=Pak4; Synonyms=Kiaa1142;
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 [MRNA], INTERACTION WITH FGFR2 AND GRB2, AND
RP PHOSPHORYLATION AT TYROSINE RESIDUES.
RC STRAIN=BALB/cJ;
RX PubMed=12529371; DOI=10.1074/jbc.m205875200;
RA Lu Y., Pan Z.-Z., Devaux Y., Ray P.;
RT "p21-activated protein kinase 4 (PAK4) interacts with the keratinocyte
RT growth factor receptor and participates in keratinocyte growth factor-
RT mediated inhibition of oxidant-induced cell death.";
RL J. Biol. Chem. 278:10374-10380(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Embryo, and Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF LIMK1.
RX PubMed=11413130; DOI=10.1074/jbc.m100871200;
RA Dan C., Kelly A., Bernard O., Minden A.;
RT "Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are
RT mediated by LIM kinase 1 and cofilin.";
RL J. Biol. Chem. 276:32115-32121(2001).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=14517283; DOI=10.1128/mcb.23.20.7122-7133.2003;
RA Qu J., Li X., Novitch B.G., Zheng Y., Kohn M., Xie J.M., Kozinn S.,
RA Bronson R., Beg A.A., Minden A.;
RT "PAK4 kinase is essential for embryonic viability and for proper neuronal
RT development.";
RL Mol. Cell. Biol. 23:7122-7133(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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 [12]
RP FUNCTION.
RX PubMed=21381077; DOI=10.1002/jcb.23092;
RA Nekrasova T., Minden A.;
RT "PAK4 is required for regulation of the cell-cycle regulatory protein p21,
RT and for control of cell-cycle progression.";
RL J. Cell. Biochem. 112:1795-1806(2011).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=21382368; DOI=10.1016/j.ydbio.2011.02.026;
RA Tian Y., Lei L., Minden A.;
RT "A key role for Pak4 in proliferation and differentiation of neural
RT progenitor cells.";
RL Dev. Biol. 353:206-216(2011).
CC -!- FUNCTION: Serine/threonine protein kinase that plays a role in a
CC variety of different signaling pathways including cytoskeleton
CC regulation, cell migration, growth, proliferation or cell survival.
CC Activation by various effectors including growth factor receptors or
CC active CDC42 and RAC1 results in a conformational change and a
CC subsequent autophosphorylation on several serine and/or threonine
CC residues. Phosphorylates and inactivates the protein phosphatase SSH1,
CC leading to increased inhibitory phosphorylation of the actin
CC binding/depolymerizing factor cofilin. Decreased cofilin activity may
CC lead to stabilization of actin filaments. Phosphorylates LIMK1, a
CC kinase that also inhibits the activity of cofilin. Phosphorylates
CC integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates
CC ARHGEF2 and activates the downstream target RHOA that plays a role in
CC the regulation of assembly of focal adhesions and actin stress fibers.
CC Stimulates cell survival by phosphorylating the BCL2 antagonist of cell
CC death BAD. Alternatively, inhibits apoptosis by preventing caspase-8
CC binding to death domain receptors in a kinase independent manner. Plays
CC a role in cell-cycle progression by controlling levels of the cell-
CC cycle regulatory protein CDKN1A and by phosphorylating RAN.
CC {ECO:0000269|PubMed:11413130, ECO:0000269|PubMed:21381077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Inhibited by INKA1; which inhibits the
CC serine/threonine-protein kinase activity by binding PAK4 in a
CC substrate-like manner. {ECO:0000250|UniProtKB:O96013}.
CC -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21
CC and weakly with RAC1 (By similarity). Interacts with FGFR2 and GRB2
CC (PubMed:12529371). Interacts with INKA1. Interacts with SH3RF2 (By
CC similarity). {ECO:0000250|UniProtKB:O96013,
CC ECO:0000269|PubMed:12529371}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O96013}.
CC Note=Seems to shuttle between cytoplasmic compartments depending on the
CC activating effector. For example, can be found on the cell periphery
CC after activation of growth-factor or integrin-mediated signaling
CC pathways. {ECO:0000250|UniProtKB:O96013}.
CC -!- PTM: Autophosphorylated on serine residues when activated by CDC42/p21
CC (By similarity). Phosphorylated on tyrosine residues upon stimulation
CC of FGFR2 (PubMed:12529371). Methylated by SETD6.
CC {ECO:0000250|UniProtKB:O96013, ECO:0000269|PubMed:12529371}.
CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000250|UniProtKB:O96013}.
CC -!- DISRUPTION PHENOTYPE: Mice die at embryonic day 11.5 probably due to a
CC defect in the fetal heart. They show strong defects in neuronal
CC development and axonal outgrowth. Spinal cord motor neurons and
CC interneurons failed to differentiate and migrate to their proper
CC position. Nervous system-specific conditional PAK4 deletion mice
CC display growth retardation and die prematurely.
CC {ECO:0000269|PubMed:14517283, ECO:0000269|PubMed:21382368}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98108.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY217016; AAO61496.1; -; mRNA.
DR EMBL; AK129298; BAC98108.2; ALT_INIT; mRNA.
DR EMBL; AK017713; BAB30889.1; -; mRNA.
DR EMBL; AK088512; BAC40396.1; -; mRNA.
DR EMBL; BC048238; AAH48238.1; -; mRNA.
DR CCDS; CCDS21049.1; -.
DR RefSeq; NP_081746.1; NM_027470.3.
DR RefSeq; XP_017167785.1; XM_017312296.1.
DR RefSeq; XP_017167786.1; XM_017312297.1.
DR AlphaFoldDB; Q8BTW9; -.
DR SMR; Q8BTW9; -.
DR BioGRID; 214149; 4.
DR iPTMnet; Q8BTW9; -.
DR PhosphoSitePlus; Q8BTW9; -.
DR EPD; Q8BTW9; -.
DR jPOST; Q8BTW9; -.
DR MaxQB; Q8BTW9; -.
DR PaxDb; Q8BTW9; -.
DR PeptideAtlas; Q8BTW9; -.
DR PRIDE; Q8BTW9; -.
DR ProteomicsDB; 294376; -.
DR Antibodypedia; 16732; 640 antibodies from 43 providers.
DR DNASU; 70584; -.
DR Ensembl; ENSMUST00000032823; ENSMUSP00000032823; ENSMUSG00000030602.
DR Ensembl; ENSMUST00000108283; ENSMUSP00000103918; ENSMUSG00000030602.
DR GeneID; 70584; -.
DR KEGG; mmu:70584; -.
DR UCSC; uc009fzh.1; mouse.
DR CTD; 10298; -.
DR MGI; MGI:1917834; Pak4.
DR VEuPathDB; HostDB:ENSMUSG00000030602; -.
DR GeneTree; ENSGT00940000159792; -.
DR HOGENOM; CLU_000288_26_6_1; -.
DR InParanoid; Q8BTW9; -.
DR OMA; QENGDPQ; -.
DR OrthoDB; 757766at2759; -.
DR PhylomeDB; Q8BTW9; -.
DR TreeFam; TF105352; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 70584; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pak4; mouse.
DR PRO; PR:Q8BTW9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BTW9; protein.
DR Bgee; ENSMUSG00000030602; Expressed in animal zygote and 218 other tissues.
DR Genevisible; Q8BTW9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0060996; P:dendritic spine development; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell cycle; Cytoplasm; Kinase; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..593
FT /note="Serine/threonine-protein kinase PAK 4"
FT /id="PRO_0000086475"
FT DOMAIN 11..24
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 323..574
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 25..322
FT /note="Linker"
FT REGION 95..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 329..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 78
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96013"
FT MOD_RES 476
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT CONFLICT 5
FT /note="K -> R (in Ref. 1; AAO61496)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="P -> L (in Ref. 1; AAO61496)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="T -> P (in Ref. 4; BAB30889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 64623 MW; 4AFA91DD73D4C6D5 CRC64;
MFGKKKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLIDPACIT
SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRESPPPPAR AHQENGMLEE
RAAPARMAPD KAGSRARATG HSEAGSGSGD RRRVGPEKRP KSSRDGPGGP QEASRDKRPL
SGPDVSTPQP GSLTSGTKLA AGRPFNTYPR ADTDHPPRGA QGEPHTMAPN GPSATGLAAP
QSSSSSRPPT RARGAPSPGV LGPHASEPQL APPARALAAP AVPPAPGPPG PRSPQREPQR
VSHEQFRAAL QLVVDPGDPR SYLDNFIKIG EGSTGIVCIA TVRSSGKLVA VKKMDLRKQQ
RRELLFNEVV IMRDYRHENV VEMYNSYLVG DELWVVMEFL EGGALTDIVT HTRMNEEQIA
AVCLAVLQAL AVLHAQGVIH RDIKSDSILL THDGRVKLSD FGFCAQVSKE VPRRKSLVGT
PYWMAPELIS RLPYGPEVDI WSLGVMVIEM VDGEPPYFNE PPLKAMKMIR DNLPPRLKNL
HKASPSLKGF LDRLLVRDPA QRATAAELLK HPFLTKAGPP ASIVPLMRQH RTR
