PHAR4_MOUSE
ID PHAR4_MOUSE Reviewed; 694 AA.
AC Q501J7; A2ALF7; A2ALG0; F6QNZ3; Q5DTM4; Q6DI97; Q8C7U9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phosphatase and actin regulator 4;
DE AltName: Full=Protein Humpty dumpty;
DE Short=Humdy;
GN Name=Phactr4; Synonyms=Kiaa4120;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 IDENTIFICATION.
RX PubMed=15107502; DOI=10.1073/pnas.0401673101;
RA Allen P.B., Greenfield A.T., Svenningsson P., Haspeslagh D.C.,
RA Greengard P.;
RT "Phactrs 1-4: a family of protein phosphatase 1 and actin regulatory
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7187-7192(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH
RP PPP1CA AND ACTIN, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS
RP OF ARG-650.
RX PubMed=17609112; DOI=10.1016/j.devcel.2007.04.018;
RA Kim T.H., Goodman J., Anderson K.V., Niswander L.;
RT "Phactr4 regulates neural tube and optic fissure closure by controlling
RT PP1-, Rb-, and E2F1-regulated cell-cycle progression.";
RL Dev. Cell 13:87-102(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-436, AND
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-264;
RP SER-285; SER-420; THR-425; SER-436; SER-446; SER-457; SER-503 AND SER-505,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22215812; DOI=10.1101/gad.179283.111;
RA Zhang Y., Kim T.H., Niswander L.;
RT "Phactr4 regulates directional migration of enteric neural crest through
RT PP1, integrin signaling, and cofilin activity.";
RL Genes Dev. 26:69-81(2012).
CC -!- FUNCTION: Regulator of protein phosphatase 1 (PP1) required for neural
CC tube and optic fissure closure, and enteric neural crest cell (ENCCs)
CC migration during development. Acts as an activator of PP1 by
CC interacting with PPP1CA and preventing phosphorylation of PPP1CA at
CC 'Thr-320'. During neural tube closure, localizes to the ventral neural
CC tube and activates PP1, leading to down-regulate cell proliferation
CC within cranial neural tissue and the neural retina. Also acts as a
CC regulator of migration of enteric neural crest cells (ENCCs) by
CC activating PP1, leading to dephosphorylation and subsequent activation
CC of cofilin (COF1 or COF2) and repression of the integrin signaling
CC through the RHO/ROCK pathway. {ECO:0000269|PubMed:17609112,
CC ECO:0000269|PubMed:22215812}.
CC -!- SUBUNIT: Binds PPP1CA and actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, lamellipodium.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q501J7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q501J7-2; Sequence=VSP_025440;
CC Name=3;
CC IsoId=Q501J7-3; Sequence=VSP_025439;
CC -!- DEVELOPMENTAL STAGE: During embryonic development, most strongly
CC expressed in neural tissue. Expressed in a dynamic pattern during
CC neurulation: from 8.5 dpc to 9.5 dpc, the period of cranial neural
CC closure and spatially regulated proliferation, it is expressed strongly
CC in the ventral region of the cranial neural tube. By 10.5 dpc,
CC expressed more uniformly along the dorsal and ventral aspects of the
CC cranial neural tube. Also expressed in the neural retina and lens.
CC {ECO:0000269|PubMed:17609112}.
CC -!- DISRUPTION PHENOTYPE: Neural tube and eye defects in embryos followed
CC by death. By 9.25 dpc, mutant embryos show failure to close the cranial
CC neural tube. About 15% of homozygous mutant embryos exhibit severe
CC exencephaly, along with a wavy spinal neural tube and a shortened
CC anterior/posterior body axis, and die around 10.5 dpc. Remaining
CC embryos exhibit complete exencephaly from the forebrain to hindbrain.
CC Most embryos die by 14.5 dpc, but a few survive to birth and die
CC shortly thereafter. Embryos also have eye defects: they display
CC overgrowth of the neural retina and retinal pigment epithelium. Embryos
CC also display coloboma at 12.5 dpc and 16.5 dpc, due to defects in
CC closure of optic fissure. Defects are due to elevated proliferation and
CC abnormally phosphorylated, inactive PP1, resulting in RB1
CC hyperphosphorylation, derepression of E2F targets, and abnormal cell-
CC cycle progression. Embryos also show embryonic gastrointestinal defects
CC due to colon hypoganglionosis, which resembles human Hirschsprung
CC disease: ENCCs within the embryonic gut display a collective cell
CC migration defect and show undirected cellular protrusions and disrupted
CC directional and chain migration. {ECO:0000269|PubMed:17609112,
CC ECO:0000269|PubMed:22215812}.
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90294.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM26520.1; Type=Erroneous gene model prediction; 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; AK049209; BAC33611.1; -; mRNA.
DR EMBL; AK220496; BAD90294.1; ALT_INIT; mRNA.
DR EMBL; AL805897; CAM26521.1; -; Genomic_DNA.
DR EMBL; AL805897; CAM26523.1; -; Genomic_DNA.
DR EMBL; AL805897; CAM26520.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC075672; AAH75672.1; -; mRNA.
DR EMBL; BC096033; AAH96033.1; -; mRNA.
DR CCDS; CCDS18724.1; -. [Q501J7-1]
DR CCDS; CCDS51318.1; -. [Q501J7-2]
DR RefSeq; NP_001155269.1; NM_001161797.1. [Q501J7-2]
DR RefSeq; NP_780515.2; NM_175306.4. [Q501J7-1]
DR RefSeq; XP_006538519.1; XM_006538456.3. [Q501J7-3]
DR AlphaFoldDB; Q501J7; -.
DR SMR; Q501J7; -.
DR BioGRID; 221393; 4.
DR STRING; 10090.ENSMUSP00000099628; -.
DR iPTMnet; Q501J7; -.
DR PhosphoSitePlus; Q501J7; -.
DR EPD; Q501J7; -.
DR jPOST; Q501J7; -.
DR MaxQB; Q501J7; -.
DR PaxDb; Q501J7; -.
DR PeptideAtlas; Q501J7; -.
DR PRIDE; Q501J7; -.
DR ProteomicsDB; 288137; -. [Q501J7-1]
DR ProteomicsDB; 288138; -. [Q501J7-2]
DR ProteomicsDB; 288139; -. [Q501J7-3]
DR Antibodypedia; 30935; 125 antibodies from 27 providers.
DR Ensembl; ENSMUST00000084170; ENSMUSP00000081185; ENSMUSG00000066043. [Q501J7-2]
DR Ensembl; ENSMUST00000084249; ENSMUSP00000081270; ENSMUSG00000066043. [Q501J7-3]
DR Ensembl; ENSMUST00000102568; ENSMUSP00000099628; ENSMUSG00000066043. [Q501J7-1]
DR GeneID; 100169; -.
DR KEGG; mmu:100169; -.
DR UCSC; uc008vbg.3; mouse. [Q501J7-1]
DR UCSC; uc008vbh.3; mouse. [Q501J7-2]
DR CTD; 65979; -.
DR MGI; MGI:2140327; Phactr4.
DR VEuPathDB; HostDB:ENSMUSG00000066043; -.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000157582; -.
DR HOGENOM; CLU_015753_1_1_1; -.
DR InParanoid; Q501J7; -.
DR OMA; XKNEADR; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; Q501J7; -.
DR TreeFam; TF316316; -.
DR BioGRID-ORCS; 100169; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Phactr4; mouse.
DR PRO; PR:Q501J7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q501J7; protein.
DR Bgee; ENSMUSG00000066043; Expressed in paneth cell and 201 other tissues.
DR ExpressionAtlas; Q501J7; baseline and differential.
DR Genevisible; Q501J7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:UniProtKB.
DR GO; GO:0072542; F:protein phosphatase activator activity; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0061386; P:closure of optic fissure; IMP:UniProtKB.
DR GO; GO:0048484; P:enteric nervous system development; IMP:UniProtKB.
DR GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:UniProtKB.
DR InterPro; IPR029984; Phactr4.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF4; PTHR12751:SF4; 1.
DR Pfam; PF02755; RPEL; 3.
DR SMART; SM00707; RPEL; 3.
DR PROSITE; PS51073; RPEL; 3.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell projection; Cytoplasm;
KW Developmental protein; Neurogenesis; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat.
FT CHAIN 1..694
FT /note="Phosphatase and actin regulator 4"
FT /id="PRO_0000287307"
FT REPEAT 63..88
FT /note="RPEL 1"
FT REPEAT 575..600
FT /note="RPEL 2"
FT REPEAT 613..638
FT /note="RPEL 3"
FT REGION 1..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 425
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT VAR_SEQ 1..5
FT /note="MEDPS -> MGQADVSRPVNPDAV (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_025439"
FT VAR_SEQ 64..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025440"
FT MUTAGEN 650
FT /note="R->P: In humdy; failure to close the neural tube and
FT optic fissure, causing exencephaly and retinal coloboma and
FT common birth defects. Specifically disrupts interaction
FT with PPP1CA while it does not affect interaction with
FT actin."
FT /evidence="ECO:0000269|PubMed:17609112"
FT CONFLICT 212
FT /note="T -> K (in Ref. 1; BAC33611)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> S (in Ref. 3; AAH96033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 694 AA; 76632 MW; 3AEB17E6A390DD29 CRC64;
MEDPSEEAEQ PSGDPGMGMD SVEAGDTTPP TKRKSKFSAL GKIFKPWKWR KKKSSDKFKE
TSEVLERKIS MRKPREELVK RGVLLEDPEQ DGEDSGKLSH AALKNGHTTP IGSARSSSPV
LVEEEPERSL RNLTPEEESK KRLGSTGSQP NSEAEPGPEH APKQPLLPPK RPLSSSCEAK
EVPAGSTARS VSSTSGSTTV TSAATTAATD MTKTVKSFVG PTPAPAPAPR TLPAAPASAN
TAATTTAPAK QPPIPPPKPA QRNSNPIIAE LSQAMNSGTV LSKPSPPLPP KRGIPSTSIP
SLEPAASFTT KTANDQREKT VSLCLEPPLI IPPSSPSPPL PTHIPPEPPR SPLVPAKTFQ
IVPEVEFSSS SDLFQDISQQ EDQKTEVPKK IQDQSFGESH IPSRLPPLPL HIRIQQALTS
PLPVTPPLEG THRAHSLLFE NSDSFSEDTG TLGRTRSLPI TIEMLKVPDD EEEEQTCPFV
EDVTSTSATP SLPLCLREEE KESDSDSEGP IKYRDEEEDD DDDESHQSAL ANRVKRKDTL
AMKLSSRPSE PETNLNSWPR KSKEEWNEIR HQIGNTLIRR LSQRPTAEEL EQRNILQPKN
EADRQAEKRE IKRRLTRKLS QRPTVAELLA RKILRFNEYV EVTDAHDYDR RADKPWTKLT
PADKAAIRKE LNEFKSSEME VHVDSKHFTR YHRP
