PHAR2_HUMAN
ID PHAR2_HUMAN Reviewed; 634 AA.
AC O75167; A6NKP5; A7MCZ5; A8MZC0; B2RWP7; B4DN76; B4DPB5; B4DTH7; Q5TFA0;
AC Q68DM2;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphatase and actin regulator 2;
GN Name=PHACTR2; Synonyms=C6orf56, KIAA0680;
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 1), AND VARIANT SER-165.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Kidney, and Placenta;
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 MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-165.
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-25; SER-522 AND
RP SER-560, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP MYRISTOYLATION AT GLY-2 (ISOFORMS 2 AND 4), CLEAVAGE OF INITIATOR
RP METHIONINE (ISOFORMS 2 AND 4), AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
CC -!- SUBUNIT: Binds PPP1CA and actin. {ECO:0000250}.
CC -!- INTERACTION:
CC O75167; P16333: NCK1; NbExp=2; IntAct=EBI-1754409, EBI-389883;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75167-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75167-2; Sequence=VSP_012272, VSP_012273;
CC Name=4;
CC IsoId=O75167-4; Sequence=VSP_012272;
CC Name=5;
CC IsoId=O75167-5; Sequence=VSP_012273;
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31655.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG60527.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014580; BAA31655.2; ALT_INIT; mRNA.
DR EMBL; AK297799; BAG60138.1; -; mRNA.
DR EMBL; AK298263; BAG60527.1; ALT_SEQ; mRNA.
DR EMBL; AK300221; BAG61989.1; -; mRNA.
DR EMBL; CR749345; CAH18198.1; -; mRNA.
DR EMBL; AL049844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150630; AAI50631.1; -; mRNA.
DR EMBL; BC152416; AAI52417.1; -; mRNA.
DR CCDS; CCDS43512.1; -. [O75167-5]
DR CCDS; CCDS47492.1; -. [O75167-1]
DR CCDS; CCDS47493.1; -. [O75167-4]
DR CCDS; CCDS47494.1; -. [O75167-2]
DR PIR; T00359; T00359.
DR RefSeq; NP_001093634.1; NM_001100164.1. [O75167-4]
DR RefSeq; NP_001093635.1; NM_001100165.1. [O75167-2]
DR RefSeq; NP_001093636.1; NM_001100166.1. [O75167-5]
DR RefSeq; NP_055536.2; NM_014721.2. [O75167-1]
DR AlphaFoldDB; O75167; -.
DR SMR; O75167; -.
DR BioGRID; 115097; 19.
DR IntAct; O75167; 18.
DR MINT; O75167; -.
DR STRING; 9606.ENSP00000417038; -.
DR GlyGen; O75167; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75167; -.
DR PhosphoSitePlus; O75167; -.
DR BioMuta; PHACTR2; -.
DR CPTAC; CPTAC-989; -.
DR EPD; O75167; -.
DR jPOST; O75167; -.
DR MassIVE; O75167; -.
DR MaxQB; O75167; -.
DR PaxDb; O75167; -.
DR PeptideAtlas; O75167; -.
DR PRIDE; O75167; -.
DR ProteomicsDB; 49831; -. [O75167-1]
DR ProteomicsDB; 49832; -. [O75167-2]
DR ProteomicsDB; 49833; -. [O75167-4]
DR ProteomicsDB; 49834; -. [O75167-5]
DR Antibodypedia; 33158; 93 antibodies from 17 providers.
DR DNASU; 9749; -.
DR Ensembl; ENST00000305766.10; ENSP00000305530.6; ENSG00000112419.15. [O75167-5]
DR Ensembl; ENST00000367582.7; ENSP00000356554.3; ENSG00000112419.15. [O75167-2]
DR Ensembl; ENST00000427704.6; ENSP00000391763.2; ENSG00000112419.15. [O75167-1]
DR Ensembl; ENST00000440869.7; ENSP00000417038.2; ENSG00000112419.15. [O75167-4]
DR GeneID; 9749; -.
DR KEGG; hsa:9749; -.
DR MANE-Select; ENST00000440869.7; ENSP00000417038.2; NM_001100164.2; NP_001093634.1. [O75167-4]
DR UCSC; uc003qjq.4; human. [O75167-1]
DR CTD; 9749; -.
DR DisGeNET; 9749; -.
DR GeneCards; PHACTR2; -.
DR HGNC; HGNC:20956; PHACTR2.
DR HPA; ENSG00000112419; Group enriched (choroid plexus, placenta).
DR MIM; 608724; gene.
DR neXtProt; NX_O75167; -.
DR OpenTargets; ENSG00000112419; -.
DR PharmGKB; PA134944445; -.
DR VEuPathDB; HostDB:ENSG00000112419; -.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000157628; -.
DR HOGENOM; CLU_015753_2_0_1; -.
DR InParanoid; O75167; -.
DR OMA; PSHKGDE; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; O75167; -.
DR TreeFam; TF316316; -.
DR PathwayCommons; O75167; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; O75167; -.
DR BioGRID-ORCS; 9749; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; PHACTR2; human.
DR GenomeRNAi; 9749; -.
DR Pharos; O75167; Tbio.
DR PRO; PR:O75167; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O75167; protein.
DR Bgee; ENSG00000112419; Expressed in placenta and 205 other tissues.
DR ExpressionAtlas; O75167; baseline and differential.
DR Genevisible; O75167; HS.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR029991; Phactr2.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF5; PTHR12751:SF5; 1.
DR Pfam; PF02755; RPEL; 2.
DR SMART; SM00707; RPEL; 4.
DR PROSITE; PS51073; RPEL; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Protein phosphatase inhibitor; Reference proteome; Repeat.
FT CHAIN 1..634
FT /note="Phosphatase and actin regulator 2"
FT /id="PRO_0000126636"
FT REPEAT 60..85
FT /note="RPEL 1"
FT REPEAT 477..502
FT /note="RPEL 2"
FT REPEAT 515..540
FT /note="RPEL 3"
FT REPEAT 553..578
FT /note="RPEL 4"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62025"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..4
FT /note="MDNA -> MGQTSVSTLSPQPGS (in isoform 2 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_012272"
FT VAR_SEQ 141..220
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_012273"
FT VARIANT 165
FT /note="P -> S (in dbSNP:rs2073214)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_045628"
FT VARIANT 449
FT /note="I -> V (in dbSNP:rs2295201)"
FT /id="VAR_053646"
FT CONFLICT 197
FT /note="T -> I (in Ref. 5; AAI50631)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="R -> K (in Ref. 2; BAG60138)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="K -> R (in Ref. 2; BAG60138)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="E -> G (in Ref. 2; BAG60138)"
FT /evidence="ECO:0000305"
FT INIT_MET O75167-2:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25807930"
FT LIPID O75167-2:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25807930"
FT INIT_MET O75167-4:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25807930"
FT LIPID O75167-4:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25807930"
SQ SEQUENCE 634 AA; 69700 MW; B45A5C5F2E389779 CRC64;
MDNAVDGLDK ASIANSDGPT AGSQTPPFKR KGKLSTIGKI FKPWKWRKKK TSDKFRETSA
VLERKISTRQ SREELIRRGV LKELPDQDGD VTVNFENSNG HMIPIGEEST REENVVKSEE
GNGSVSEKTP PLEEQAEDKK ENTENHSETP AAPALPPSAP PKPRPKPKPK KSPVPPKGAT
AGASHKGDEV PPIKKNTKAP GKQAPVPPPK PASRNTTREA AGSSHSKKTT GSKASASPST
SSTSSRPKAS KETVSSKAGT VGTTKGKRKT DKQPITSHLS SDTTTSGTSD LKGEPAETRV
ESFKLEQTVP GAEEQNTGKF KSMVPPPPVA PAPSPLAPPL PLEDQCITAS DTPVVLVSVG
ADLPVSALDP SQLLWAEEPT NRTTLYSGTG LSVNRENAKC FTTKEELGKT VPQLLTPGLM
GESSESFSAS EDEGHREYQA NDSDSDGPIL YTDDEDEDED EDGSGESALA SKIRRRDTLA
IKLGNRPSKK ELEDKNILQR TSEEERQEIR QQIGTKLVRR LSQRPTTEEL EQRNILKQKN
EEEEQEAKME LKRRLSRKLS LRPTVAELQA RRILRFNEYV EVTDSPDYDR RADKPWARLT
PADKAAIRKE LNEFKSTEME VHEESRQFTR FHRP
