PHAR1_MOUSE
ID PHAR1_MOUSE Reviewed; 580 AA.
AC Q2M3X8; B1B1B5; B1B1B6; B1B1B7; G5E8P7; Q80VL9; Q8C873;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphatase and actin regulator 1;
GN Name=Phactr1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum;
RX PubMed=16359841; DOI=10.1016/j.ygeno.2005.10.009;
RA de Chaldee M., Brochier C., Van de Vel A., Caudy N., Luthi-Carter R.,
RA Gaillard M.-C., Elalouf J.-M.;
RT "Capucin: a novel striatal marker down-regulated in rodent models of
RT Huntington disease.";
RL Genomics 87:200-207(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 4).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Eye, and Olfactory epithelium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-580 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-78 AND THR-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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 [7]
RP FUNCTION, INTERACTION WITH PPP1CA AND ACTA1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 108-ARG--LYS-129; ARG-147; ARG-431; ARG-469 AND ARG-507.
RX PubMed=22976292; DOI=10.1242/jcs.112078;
RA Wiezlak M., Diring J., Abella J., Mouilleron S., Way M., McDonald N.Q.,
RA Treisman R.;
RT "G-actin regulates the shuttling and PP1 binding of the RPEL protein
RT Phactr1 to control actomyosin assembly.";
RL J. Cell Sci. 125:5860-5872(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASN-479; LEU-500;
RP ILE-518 AND ARG-521.
RX PubMed=30256902; DOI=10.1093/brain/awy246;
RA Hamada N., Ogaya S., Nakashima M., Nishijo T., Sugawara Y., Iwamoto I.,
RA Ito H., Maki Y., Shirai K., Baba S., Maruyama K., Saitsu H., Kato M.,
RA Matsumoto N., Momiyama T., Nagata K.I.;
RT "De novo PHACTR1 mutations in West syndrome and their pathophysiological
RT effects.";
RL Brain 141:3098-3114(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 133-164 AND 414-528 IN COMPLEXES
RP WITH ACTA1, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF
RP GLY-459; ILE-496 AND ARG-516, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23041370; DOI=10.1016/j.str.2012.08.031;
RA Mouilleron S., Wiezlak M., O'Reilly N., Treisman R., McDonald N.Q.;
RT "Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-
RT actin reveal the molecular basis for actin binding cooperativity.";
RL Structure 20:1960-1970(2012).
CC -!- FUNCTION: Binds actin monomers (G actin) and plays a role in multiple
CC processes including the regulation of actin cytoskeleton dynamics,
CC actin stress fibers formation, cell motility and survival, formation of
CC tubules by endothelial cells, and regulation of PPP1CA activity.
CC Involved in the regulation of cortical neuron migration and dendrite
CC arborization (PubMed:30256902). {ECO:0000250,
CC ECO:0000269|PubMed:22976292, ECO:0000269|PubMed:23041370,
CC ECO:0000269|PubMed:30256902}.
CC -!- SUBUNIT: Interacts (via RPEL repeats) with ACTA1 and PPP1CA; ACTA1 and
CC PPP1CA compete for the same binding site. {ECO:0000269|PubMed:22976292,
CC ECO:0000269|PubMed:23041370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Synapse {ECO:0000250}. Nucleus.
CC Note=Enriched at synapses (By similarity). Cytoplasmic in resting
CC cells, and is imported into the nucleus upon serum stimulation.
CC Interaction with actin prevents nuclear import. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q2M3X8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M3X8-2; Sequence=VSP_018559;
CC Name=3;
CC IsoId=Q2M3X8-3; Sequence=VSP_018559, VSP_018560;
CC Name=4;
CC IsoId=Q2M3X8-4; Sequence=VSP_018560;
CC -!- DOMAIN: Binds three actin monomers via the three C-terminal RPEL
CC repeats. {ECO:0000269|PubMed:23041370}.
CC -!- DISRUPTION PHENOTYPE: PHACTR1 knockdown results in migration defects of
CC cortical neurons. Neurons do not migrate to layers II-IV of the
CC cortical plate but remain in the lower part and the intermediate zone.
CC {ECO:0000269|PubMed:30256902}.
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48407.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH61691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC33272.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY993932; AAY42814.1; -; mRNA.
DR EMBL; AC140415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC164878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466546; EDL40986.1; -; Genomic_DNA.
DR EMBL; BC048407; AAH48407.1; ALT_INIT; mRNA.
DR EMBL; BC061691; AAH61691.1; ALT_INIT; mRNA.
DR EMBL; AK048208; BAC33272.1; ALT_INIT; mRNA.
DR CCDS; CCDS49251.1; -. [Q2M3X8-3]
DR CCDS; CCDS79181.1; -. [Q2M3X8-1]
DR RefSeq; NP_001005740.1; NM_001005740.1. [Q2M3X8-3]
DR RefSeq; NP_001289564.1; NM_001302635.1. [Q2M3X8-1]
DR RefSeq; NP_001289565.1; NM_001302636.1.
DR RefSeq; XP_006516968.1; XM_006516905.3. [Q2M3X8-4]
DR RefSeq; XP_006516969.1; XM_006516906.3. [Q2M3X8-4]
DR RefSeq; XP_011242697.1; XM_011244395.2. [Q2M3X8-4]
DR RefSeq; XP_017170971.1; XM_017315482.1.
DR RefSeq; XP_017170972.1; XM_017315483.1.
DR PDB; 4B1U; X-ray; 2.00 A; M=133-164.
DR PDB; 4B1V; X-ray; 1.75 A; M/N=133-164.
DR PDB; 4B1W; X-ray; 1.95 A; M=417-448.
DR PDB; 4B1X; X-ray; 1.80 A; M=455-486.
DR PDB; 4B1Y; X-ray; 1.29 A; M=493-524.
DR PDB; 4B1Z; X-ray; 3.30 A; M/N=414-528.
DR PDBsum; 4B1U; -.
DR PDBsum; 4B1V; -.
DR PDBsum; 4B1W; -.
DR PDBsum; 4B1X; -.
DR PDBsum; 4B1Y; -.
DR PDBsum; 4B1Z; -.
DR AlphaFoldDB; Q2M3X8; -.
DR SMR; Q2M3X8; -.
DR BioGRID; 229998; 5.
DR IntAct; Q2M3X8; 4.
DR MINT; Q2M3X8; -.
DR iPTMnet; Q2M3X8; -.
DR PhosphoSitePlus; Q2M3X8; -.
DR jPOST; Q2M3X8; -.
DR MaxQB; Q2M3X8; -.
DR PeptideAtlas; Q2M3X8; -.
DR PRIDE; Q2M3X8; -.
DR ProteomicsDB; 289484; -. [Q2M3X8-1]
DR ProteomicsDB; 289485; -. [Q2M3X8-2]
DR ProteomicsDB; 289486; -. [Q2M3X8-3]
DR ProteomicsDB; 289487; -. [Q2M3X8-4]
DR Antibodypedia; 24916; 66 antibodies from 20 providers.
DR DNASU; 218194; -.
DR Ensembl; ENSMUST00000066928; ENSMUSP00000066663; ENSMUSG00000054728. [Q2M3X8-2]
DR Ensembl; ENSMUST00000110161; ENSMUSP00000105790; ENSMUSG00000054728. [Q2M3X8-4]
DR Ensembl; ENSMUST00000128646; ENSMUSP00000122232; ENSMUSG00000054728. [Q2M3X8-1]
DR Ensembl; ENSMUST00000148891; ENSMUSP00000115228; ENSMUSG00000054728. [Q2M3X8-3]
DR Ensembl; ENSMUST00000149235; ENSMUSP00000115207; ENSMUSG00000054728. [Q2M3X8-1]
DR GeneID; 218194; -.
DR KEGG; mmu:218194; -.
DR UCSC; uc007qfo.2; mouse. [Q2M3X8-1]
DR UCSC; uc007qfp.1; mouse. [Q2M3X8-3]
DR UCSC; uc007qfq.1; mouse. [Q2M3X8-2]
DR CTD; 221692; -.
DR MGI; MGI:2659021; Phactr1.
DR VEuPathDB; HostDB:ENSMUSG00000054728; -.
DR GeneTree; ENSGT00940000155842; -.
DR HOGENOM; CLU_015753_3_0_1; -.
DR InParanoid; Q2M3X8; -.
DR OMA; DPGAPMK; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; Q2M3X8; -.
DR TreeFam; TF316316; -.
DR BioGRID-ORCS; 218194; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Phactr1; mouse.
DR PRO; PR:Q2M3X8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q2M3X8; protein.
DR Bgee; ENSMUSG00000054728; Expressed in nucleus accumbens and 217 other tissues.
DR ExpressionAtlas; Q2M3X8; baseline and differential.
DR Genevisible; Q2M3X8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0048870; P:cell motility; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0140059; P:dendrite arborization; IMP:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; ISO:MGI.
DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR InterPro; IPR029987; Phactr1.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF6; PTHR12751:SF6; 2.
DR Pfam; PF02755; RPEL; 4.
DR SMART; SM00707; RPEL; 4.
DR PROSITE; PS51073; RPEL; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Protein phosphatase inhibitor; Reference proteome; Repeat;
KW Synapse.
FT CHAIN 1..580
FT /note="Phosphatase and actin regulator 1"
FT /id="PRO_0000235990"
FT REPEAT 138..163
FT /note="RPEL 1"
FT REPEAT 422..447
FT /note="RPEL 2"
FT REPEAT 460..485
FT /note="RPEL 3"
FT REPEAT 498..523
FT /note="RPEL 4"
FT REGION 330..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..129
FT /note="Nuclear localization signal"
FT COMPBIAS 330..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D0"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D0"
FT VAR_SEQ 1..34
FT /note="MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQ -> MCVSLLLSPPPPFR
FT LSPSPSLHLLLLS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018559"
FT VAR_SEQ 221
FT /note="P -> PVSEESPSASESGVLLSQDPSAKPVLFLPPKKSAAFPGDHEETPVKQ
FT LSLHKQPPALPPKPTARIANHLT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018560"
FT MUTAGEN 108..110
FT /note="RRR->AAA: Abolishes nuclear import."
FT MUTAGEN 127..129
FT /note="KKK->AAA: Abolishes nuclear import."
FT MUTAGEN 147
FT /note="R->A: Reduces affinity for actin."
FT /evidence="ECO:0000269|PubMed:22976292"
FT MUTAGEN 431
FT /note="R->A: Constitutively nuclear; when associated with
FT A-469 and A-507. Strongly reduced affinity for actin."
FT /evidence="ECO:0000269|PubMed:22976292"
FT MUTAGEN 459
FT /note="G->K: Increases affinity for actin."
FT /evidence="ECO:0000269|PubMed:23041370"
FT MUTAGEN 469
FT /note="R->A: Constitutively nuclear; when associated with
FT A-431 and A-507. Strongly reduced affinity for actin."
FT /evidence="ECO:0000269|PubMed:22976292"
FT MUTAGEN 479
FT /note="N->I: Does not rescue cortical neuron migration
FT defects in PHACTR1 knocked-down mice."
FT /evidence="ECO:0000269|PubMed:30256902"
FT MUTAGEN 496
FT /note="I->A: Reduces affinity for actin."
FT /evidence="ECO:0000269|PubMed:23041370"
FT MUTAGEN 500
FT /note="L->P: Does not rescue cortical neuron migration
FT defects in PHACTR1 knocked-down mice."
FT /evidence="ECO:0000269|PubMed:30256902"
FT MUTAGEN 507
FT /note="R->A: Constitutively nuclear; when associated with
FT A-431 and A-469. Strongly reduced affinity for actin."
FT /evidence="ECO:0000269|PubMed:22976292"
FT MUTAGEN 516
FT /note="R->A: Reduces affinity for actin."
FT /evidence="ECO:0000269|PubMed:23041370"
FT MUTAGEN 518
FT /note="I->N: Does not rescue cortical neuron migration
FT defects in PHACTR1 knocked-down mice."
FT /evidence="ECO:0000269|PubMed:30256902"
FT MUTAGEN 521
FT /note="R->C: Does not rescue cortical neuron migration
FT defects in PHACTR1 knocked-down mice."
FT /evidence="ECO:0000269|PubMed:30256902"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:4B1V"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:4B1V"
FT HELIX 422..429
FT /evidence="ECO:0007829|PDB:4B1W"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:4B1W"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:4B1W"
FT HELIX 458..467
FT /evidence="ECO:0007829|PDB:4B1X"
FT HELIX 472..477
FT /evidence="ECO:0007829|PDB:4B1X"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:4B1Y"
SQ SEQUENCE 580 AA; 66286 MW; 367DD2393117EC89 CRC64;
MDYPKMDYFL DVESAHRLLD VESAQRFFYS QGAQARRATL LLPPTLMAAS SEDDIDRRPI
RRVRSKSDTP YLAEARISFN LGAAEEVERL AAMRSDSLVP GTHTPPIRRR SKFANLGRIF
KPWKWRKKKS EKFKHTSAAL ERKISMRQSR EELIKRGVLK EIYDKDGELS ISNEDDSLEN
GQSLSSSQLS LPALSEMEPV PMPRDPCSYE VLQASDIMDG PDPGAPVKLP CLPVKLSPPL
PPKKVLICMP VGGPELTLAS YAAQKSSQQA VAQHHHTVLP SQMQHQLQYG SHGQHLPSST
GTLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSSDG ITKAGPMGLP
EIRQVPTVVI ECDDNKENVP HEPDYEDSPC LYGREEEEEE EDEDDDASLY TSSLAMKVCR
KDSLAIKLSN RPSKRELEEK NILPRQTDEE RLELRQQIGT KLTRRLSQRP TAEELEQRNI
LKPRNEQEEQ EEKREIKRRL TRKLSQRPTV EELRERKILI RFSDYVEVAD AQDYDRRADK
PWTRLTAADK AAIRKELNEF KSTEMEVHEL SRHLTRFHRP
