ID PHAR1_HUMAN Reviewed; 580 AA. AC Q9C0D0; A8K1V2; Q3MJ93; Q5JSJ2; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 3. DT 24-JAN-2024, entry version 155. DE RecName: Full=Phosphatase and actin regulator 1; GN Name=PHACTR1; Synonyms=KIAA1733, RPEL1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11214970; DOI=10.1093/dnares/7.6.347; RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:347-355(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala, and Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; 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 FUNCTION, AND INDUCTION. RX PubMed=21798305; DOI=10.1016/j.biochi.2011.07.010; RA Jarray R., Allain B., Borriello L., Biard D., Loukaci A., Larghero J., RA Hadj-Slimane R., Garbay C., Lepelletier Y., Raynaud F.; RT "Depletion of the novel protein PHACTR-1 from human endothelial cells RT abolishes tube formation and induces cell death receptor apoptosis."; RL Biochimie 93:1668-1675(2011). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=21939755; DOI=10.1016/j.cellsig.2011.09.003; RA Allain B., Jarray R., Borriello L., Leforban B., Dufour S., Liu W.Q., RA Pamonsinlapatham P., Bianco S., Larghero J., Hadj-Slimane R., Garbay C., RA Raynaud F., Lepelletier Y.; RT "Neuropilin-1 regulates a new VEGF-induced gene, Phactr-1, which controls RT tubulogenesis and modulates lamellipodial dynamics in human endothelial RT cells."; RL Cell. Signal. 24:214-223(2012). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 AND SER-505, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [8] RP INVOLVEMENT IN DEE70, VARIANTS DEE70 ILE-479 AND PRO-500, AND RP CHARACTERIZATION OF VARIANTS DEE70 ILE-479; PRO-500 AND CYS-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 VARIANT DEE70 CYS-521. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(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 (PubMed:21798305, PubMed:21939755). Involved in the regulation of CC cortical neuron migration and dendrite arborization (By similarity). CC {ECO:0000250|UniProtKB:Q2M3X8, ECO:0000269|PubMed:21798305, CC ECO:0000269|PubMed:21939755}. CC -!- SUBUNIT: Interacts (via RPEL repeats) with ACTA1 and PPP1CA; ACTA1 and CC PPP1CA compete for the same binding site. CC -!- INTERACTION: CC Q9C0D0; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-7971325, EBI-725606; CC Q9C0D0; Q9HC52: CBX8; NbExp=3; IntAct=EBI-7971325, EBI-712912; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. CC Nucleus {ECO:0000250}. Note=Enriched at synapses (By similarity). CC Cytoplasmic in resting cells, and is imported into the nucleus upon CC serum stimulation. Interaction with actin prevents nuclear import (By CC similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9C0D0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9C0D0-2; Sequence=VSP_018529, VSP_018530; CC -!- TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells. CC {ECO:0000269|PubMed:21939755}. CC -!- INDUCTION: Up-regulated by VEGFA. {ECO:0000269|PubMed:21798305, CC ECO:0000269|PubMed:21939755}. CC -!- DOMAIN: Binds three actin monomers via the three C-terminal RPEL CC repeats. {ECO:0000250}. CC -!- DISEASE: Developmental and epileptic encephalopathy 70 (DEE70) CC [MIM:618298]: A form of epileptic encephalopathy, a heterogeneous group CC of severe early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. DEE70 is an autosomal dominant form with onset in CC first months of life and variable severity. CC {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:30256902}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB21824.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB051520; BAB21824.1; ALT_INIT; mRNA. DR EMBL; AK090769; BAG52223.1; -; mRNA. DR EMBL; AK290017; BAF82706.1; -; mRNA. DR EMBL; AL008729; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL354680; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL591682; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z99495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC101526; AAI01527.1; -; mRNA. DR EMBL; BC101528; AAI01529.1; -; mRNA. DR CCDS; CCDS75401.1; -. [Q9C0D0-1] DR RefSeq; NP_001229577.1; NM_001242648.2. [Q9C0D0-1] DR RefSeq; NP_001309237.1; NM_001322308.1. [Q9C0D0-1] DR RefSeq; NP_001309238.1; NM_001322309.1. [Q9C0D0-1] DR RefSeq; NP_001309239.1; NM_001322310.1. DR RefSeq; NP_001309240.1; NM_001322311.1. DR RefSeq; NP_001309241.1; NM_001322312.1. DR RefSeq; NP_001309242.1; NM_001322313.1. DR RefSeq; NP_001309243.1; NM_001322314.1. DR RefSeq; NP_112210.1; NM_030948.3. [Q9C0D0-1] DR PDB; 6ZEE; X-ray; 1.90 A; C/D/U/V/W/X=508-580. DR PDB; 6ZEF; X-ray; 1.94 A; C/D=516-580. DR PDB; 6ZEG; X-ray; 1.09 A; C/D=516-580. DR PDB; 6ZEH; X-ray; 1.30 A; C/D=516-580. DR PDB; 6ZEI; X-ray; 1.39 A; C/D=516-580. DR PDB; 6ZEJ; X-ray; 1.78 A; A/D/F/I/L/O=526-580. DR PDBsum; 6ZEE; -. DR PDBsum; 6ZEF; -. DR PDBsum; 6ZEG; -. DR PDBsum; 6ZEH; -. DR PDBsum; 6ZEI; -. DR PDBsum; 6ZEJ; -. DR AlphaFoldDB; Q9C0D0; -. DR SMR; Q9C0D0; -. DR BioGRID; 128746; 8. DR IntAct; Q9C0D0; 5. DR MINT; Q9C0D0; -. DR STRING; 9606.ENSP00000329880; -. DR iPTMnet; Q9C0D0; -. DR PhosphoSitePlus; Q9C0D0; -. DR BioMuta; PHACTR1; -. DR DMDM; 97536946; -. DR EPD; Q9C0D0; -. DR jPOST; Q9C0D0; -. DR MassIVE; Q9C0D0; -. DR MaxQB; Q9C0D0; -. DR PaxDb; 9606-ENSP00000329880; -. DR PeptideAtlas; Q9C0D0; -. DR ProteomicsDB; 80005; -. [Q9C0D0-1] DR ProteomicsDB; 80006; -. [Q9C0D0-2] DR TopDownProteomics; Q9C0D0-2; -. [Q9C0D0-2] DR Antibodypedia; 24916; 71 antibodies from 21 providers. DR DNASU; 221692; -. DR Ensembl; ENST00000332995.12; ENSP00000329880.8; ENSG00000112137.19. [Q9C0D0-1] DR Ensembl; ENST00000674637.1; ENSP00000501634.1; ENSG00000112137.19. [Q9C0D0-1] DR Ensembl; ENST00000676159.1; ENSP00000501921.1; ENSG00000112137.19. [Q9C0D0-1] DR GeneID; 221692; -. DR KEGG; hsa:221692; -. DR MANE-Select; ENST00000332995.12; ENSP00000329880.8; NM_030948.6; NP_112210.1. DR UCSC; uc003nag.3; human. [Q9C0D0-1] DR AGR; HGNC:20990; -. DR CTD; 221692; -. DR DisGeNET; 221692; -. DR GeneCards; PHACTR1; -. DR HGNC; HGNC:20990; PHACTR1. DR HPA; ENSG00000112137; Tissue enhanced (bone marrow, brain). DR MalaCards; PHACTR1; -. DR MIM; 608723; gene. DR MIM; 618298; phenotype. DR neXtProt; NX_Q9C0D0; -. DR OpenTargets; ENSG00000112137; -. DR Orphanet; 3451; Infantile spasms syndrome. DR PharmGKB; PA134923900; -. DR VEuPathDB; HostDB:ENSG00000112137; -. DR eggNOG; KOG4339; Eukaryota. DR GeneTree; ENSGT00940000155842; -. DR InParanoid; Q9C0D0; -. DR OrthoDB; 2882458at2759; -. DR PhylomeDB; Q9C0D0; -. DR PathwayCommons; Q9C0D0; -. DR SignaLink; Q9C0D0; -. DR SIGNOR; Q9C0D0; -. DR BioGRID-ORCS; 221692; 9 hits in 393 CRISPR screens. DR ChiTaRS; PHACTR1; human. DR GenomeRNAi; 221692; -. DR Pharos; Q9C0D0; Tbio. DR PRO; PR:Q9C0D0; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9C0D0; Protein. DR Bgee; ENSG00000112137; Expressed in cortical plate and 135 other cell types or tissues. DR ExpressionAtlas; Q9C0D0; baseline and differential. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB. DR GO; GO:0048870; P:cell motility; IMP:UniProtKB. DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB. DR GO; GO:0140059; P:dendrite arborization; ISS:UniProtKB. DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB. DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB. DR Gene3D; 6.10.140.1750; -; 1. DR Gene3D; 6.10.140.2130; -; 1. DR InterPro; IPR004018; RPEL_repeat. DR PANTHER; PTHR12751:SF6; PHOSPHATASE AND ACTIN REGULATOR 1; 1. DR PANTHER; PTHR12751; PHOSPHATASE AND ACTIN REGULATOR PHACTR; 1. DR Pfam; PF02755; RPEL; 4. DR SMART; SM00707; RPEL; 4. DR PROSITE; PS51073; RPEL; 4. DR Genevisible; Q9C0D0; HS. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Epilepsy; KW Nucleus; Phosphoprotein; Protein phosphatase inhibitor; Reference proteome; KW Repeat; Synapse. FT CHAIN 1..580 FT /note="Phosphatase and actin regulator 1" FT /id="PRO_0000126634" FT REPEAT 138..163 FT /note="RPEL 1" FT REPEAT 422..447 FT /note="RPEL 2" FT REPEAT 460..484 FT /note="RPEL 3" FT REPEAT 498..523 FT /note="RPEL 4" FT REGION 331..355 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 376..410 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 462..494 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 108..129 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 331..346 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 376..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:0000250|UniProtKB:Q2M3X8" FT MOD_RES 78 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q2M3X8" FT MOD_RES 104 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q2M3X8" FT MOD_RES 467 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 483..484 FT /note="PR -> RK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11214970" FT /id="VSP_018529" FT VAR_SEQ 485..580 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11214970" FT /id="VSP_018530" FT VARIANT 247 FT /note="I -> M (in dbSNP:rs17602409)" FT /id="VAR_053645" FT VARIANT 479 FT /note="N -> I (in DEE70; severely impaired interaction with FT actin; dbSNP:rs1562103192)" FT /evidence="ECO:0000269|PubMed:30256902" FT /id="VAR_081810" FT VARIANT 500 FT /note="L -> P (in DEE70; severely impaired interaction with FT actin; dbSNP:rs1562114406)" FT /evidence="ECO:0000269|PubMed:30256902" FT /id="VAR_081811" FT VARIANT 521 FT /note="R -> C (in DEE70; loss of interaction with PP1 FT complex; dbSNP:rs748743403)" FT /evidence="ECO:0000269|PubMed:23033978, FT ECO:0000269|PubMed:30256902" FT /id="VAR_069379" FT STRAND 527..530 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 541..543 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 547..563 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 569..574 FT /evidence="ECO:0007829|PDB:6ZEG" SQ SEQUENCE 580 AA; 66308 MW; 5111973836BBEA39 CRC64; MDYPKMDYFL DVESAHRLLD VESAQRFFYS QGAQARRATL LLPPTLMAAS SEDDIDRRPI RRVRSKSDTP YLAEARISFN LGAAEEVERL AAMRSDSLVP GTHTPPIRRR SKFANLGRIF KPWKWRKKKS EKFKHTSAAL ERKISMRQSR EELIKRGVLK EIYDKDGELS ISNEEDSLEN GQSLSSSQLS LPALSEMEPV PMPRDPCSYE VLQPSDIMDG PDPGAPVKLP CLPVKLSPPL PPKKVMICMP VGGPDLSLVS YTAQKSGQQG VAQHHHTVLP SQIQHQLQYG SHGQHLPSTT GSLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSGDG VTKAGPMGLP EIRQVPTVVI ECDDNKENVP HESDYEDSSC LYTREEEEEE EDEDDDSSLY TSSLAMKVCR KDSLAIKLSN RPSKRELEEK NILPRQTDEE RLELRQQIGT KLTRRLSQRP TAEELEQRNI LKPRNEQEEQ EEKREIKRRL TRKLSQRPTV EELRERKILI RFSDYVEVAD AQDYDRRADK PWTRLTAADK AAIRKELNEF KSTEMEVHEL SRHLTRFHRP //