PSD1_MOUSE
ID PSD1_MOUSE Reviewed; 1024 AA.
AC Q5DTT2; B2RS07; B7ZNN7; Q3TY69; Q6PE10;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=PH and SEC7 domain-containing protein 1;
DE AltName: Full=Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6;
DE Short=Exchange factor for ARF6;
DE AltName: Full=Exchange factor for ARF6 A;
DE AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 1;
GN Name=Psd; Synonyms=Efa6a, Kiaa2011, Psd1;
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), INTERACTION WITH ACTN1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=17298598; DOI=10.1111/j.1460-9568.2007.05345.x;
RA Sakagami H., Honma T., Sukegawa J., Owada Y., Yanagisawa T., Kondo H.;
RT "Somatodendritic localization of EFA6A, a guanine nucleotide exchange
RT factor for ADP-ribosylation factor 6, and its possible interaction with
RT alpha-actinin in dendritic spines.";
RL Eur. J. Neurosci. 25:618-628(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLU-621.
RC TISSUE=Brain, and Embryo;
RX PubMed=19494129; DOI=10.1242/jcs.042325;
RA Sironi C., Teesalu T., Muggia A., Fontana G., Marino F., Savaresi S.,
RA Talarico D.;
RT "EFA6A encodes two isoforms with distinct biological activities in neuronal
RT cells.";
RL J. Cell Sci. 122:2108-2118(2009).
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 2).
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
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] (ISOFORMS 1 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 805-1024 (ISOFORMS 1/2/3).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-1024 (ISOFORM 1).
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 [7]
RP INTERACTION WITH KCNK1, AND SUBCELLULAR LOCATION.
RX PubMed=15540117; DOI=10.1038/sj.embor.7400292;
RA Decressac S., Franco M., Bendahhou S., Warth R., Knauer S., Barhanin J.,
RA Lazdunski M., Lesage F.;
RT "ARF6-dependent interaction of the TWIK1 K+ channel with EFA6, a GDP/GTP
RT exchange factor for ARF6.";
RL EMBO Rep. 5:1171-1175(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-156 AND SER-720, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Guanine nucleotide exchange factor for ARF6 (By similarity).
CC Isoform 2 and isoform 3 induce cytoskeletal remodeling, but lead to
CC distinct morphological changes in HeLa cells: isoform 2 induces cell
CC elongation and formation of actin-rich protrusions, whereas isoform 3
CC promotes the formation of membrane ruffles and loss of stress fibers
CC (PubMed:19494129). {ECO:0000250|UniProtKB:A5PKW4,
CC ECO:0000269|PubMed:19494129}.
CC -!- SUBUNIT: Interacts with ACTN1 (PubMed:17298598). Interacts (ARF6-bound
CC form) with KCNK1; does not interact with KCNK1 in the absence of ARF6
CC (PubMed:15540117). {ECO:0000269|PubMed:15540117,
CC ECO:0000269|PubMed:17298598}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:17298598}. Cell
CC projection, ruffle {ECO:0000269|PubMed:15540117,
CC ECO:0000269|PubMed:17298598}. Note=Colocalizes with ACTN1 in membrane
CC ruffles and central reticular structures. {ECO:0000269|PubMed:15540117,
CC ECO:0000269|PubMed:17298598}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:19494129}. Cell projection
CC {ECO:0000269|PubMed:19494129}. Note=Accumulates in microvilli-like
CC protrusions. {ECO:0000269|PubMed:19494129}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:19494129}. Cell
CC projection, ruffle {ECO:0000269|PubMed:15540117,
CC ECO:0000269|PubMed:19494129}. Note=Colocalizes with F-actin in membrane
CC ruffles. {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:19494129}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A5PKW4}.
CC Cell projection, ruffle membrane {ECO:0000250|UniProtKB:A5PKW4}.
CC Cleavage furrow {ECO:0000250|UniProtKB:A5PKW4}. Note=Distributed
CC uniformly on the plasma membrane, as well as throughout the cytoplasm
CC during metaphase. Subsequently concentrated at patches in the
CC equatorial region at the onset of cytokinesis, and becomes distributed
CC in the equatorial region concurrent with cleavage furrow ingression. In
CC later cytokinesis phases, fades away from the cleavage furrow and
CC becomes uniformly distributed throughout the plasma membrane.
CC {ECO:0000250|UniProtKB:A5PKW4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5DTT2-1; Sequence=Displayed;
CC Name=2; Synonyms=EFA6As;
CC IsoId=Q5DTT2-2; Sequence=VSP_033637, VSP_033638;
CC Name=3; Synonyms=EFA6A;
CC IsoId=Q5DTT2-3; Sequence=VSP_041569;
CC -!- TISSUE SPECIFICITY: Highest expression detected in brain and some
CC expression detected also in uterus, stomach, ovary and intestine, with
CC isoform 2 being expressed at the highest levels. In the brain, isoform
CC 1 is highly expressed in the strata oriens, radiatum, lacunosum-
CC moleculare of the hippocampal CA1-3 regions and the dentate molecular
CC layer of the hippocampal formation, with lower levels detected in the
CC neuronal cell layers and the stratum lucidum (at protein level). Not
CC detected in tongue, thymus, spleen, lung, heart, liver and kidney.
CC {ECO:0000269|PubMed:17298598, ECO:0000269|PubMed:19494129}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic, early postnatal and adult
CC brain, with expression up-regulated at postnatal day 4-8 and down-
CC regulated in adults. Isoform 2 expression is up-regulated in adults.
CC {ECO:0000269|PubMed:19494129}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PSD family. {ECO:0000305}.
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DR EMBL; AC114539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK158851; BAE34694.1; -; mRNA.
DR EMBL; BC058352; AAH58352.1; -; mRNA.
DR EMBL; BC138652; AAI38653.1; -; mRNA.
DR EMBL; BC145352; AAI45353.1; -; mRNA.
DR EMBL; AK220438; BAD90268.1; -; Transcribed_RNA.
DR CCDS; CCDS29875.1; -. [Q5DTT2-1]
DR CCDS; CCDS84449.1; -. [Q5DTT2-3]
DR RefSeq; NP_001334383.1; NM_001347454.1. [Q5DTT2-3]
DR RefSeq; NP_082903.2; NM_028627.2. [Q5DTT2-1]
DR RefSeq; XP_006527449.1; XM_006527386.3. [Q5DTT2-3]
DR RefSeq; XP_006527451.1; XM_006527388.3. [Q5DTT2-3]
DR RefSeq; XP_006527452.1; XM_006527389.3. [Q5DTT2-3]
DR RefSeq; XP_006527454.1; XM_006527391.3. [Q5DTT2-3]
DR RefSeq; XP_006527456.1; XM_006527393.2. [Q5DTT2-2]
DR RefSeq; XP_011245678.1; XM_011247376.2. [Q5DTT2-3]
DR RefSeq; XP_011245679.1; XM_011247377.2. [Q5DTT2-1]
DR AlphaFoldDB; Q5DTT2; -.
DR SMR; Q5DTT2; -.
DR BioGRID; 216216; 3.
DR CORUM; Q5DTT2; -.
DR IntAct; Q5DTT2; 1.
DR STRING; 10090.ENSMUSP00000093729; -.
DR ChEMBL; CHEMBL4523322; -.
DR iPTMnet; Q5DTT2; -.
DR PhosphoSitePlus; Q5DTT2; -.
DR SwissPalm; Q5DTT2; -.
DR MaxQB; Q5DTT2; -.
DR PaxDb; Q5DTT2; -.
DR PeptideAtlas; Q5DTT2; -.
DR PRIDE; Q5DTT2; -.
DR ProteomicsDB; 301857; -. [Q5DTT2-1]
DR ProteomicsDB; 301858; -. [Q5DTT2-2]
DR ProteomicsDB; 301859; -. [Q5DTT2-3]
DR Antibodypedia; 31428; 54 antibodies from 17 providers.
DR DNASU; 73728; -.
DR Ensembl; ENSMUST00000041391; ENSMUSP00000039728; ENSMUSG00000037126. [Q5DTT2-1]
DR Ensembl; ENSMUST00000096029; ENSMUSP00000093729; ENSMUSG00000037126. [Q5DTT2-3]
DR Ensembl; ENSMUST00000224556; ENSMUSP00000153381; ENSMUSG00000037126. [Q5DTT2-2]
DR Ensembl; ENSMUST00000225323; ENSMUSP00000152942; ENSMUSG00000037126. [Q5DTT2-3]
DR GeneID; 73728; -.
DR KEGG; mmu:73728; -.
DR UCSC; uc008htb.1; mouse. [Q5DTT2-2]
DR UCSC; uc008htd.1; mouse. [Q5DTT2-1]
DR UCSC; uc012bmt.1; mouse. [Q5DTT2-3]
DR CTD; 5662; -.
DR MGI; MGI:1920978; Psd.
DR VEuPathDB; HostDB:ENSMUSG00000037126; -.
DR eggNOG; KOG0932; Eukaryota.
DR GeneTree; ENSGT00940000155061; -.
DR HOGENOM; CLU_011021_3_0_1; -.
DR InParanoid; Q5DTT2; -.
DR OMA; HEPASLI; -.
DR OrthoDB; 301851at2759; -.
DR PhylomeDB; Q5DTT2; -.
DR TreeFam; TF319755; -.
DR BioGRID-ORCS; 73728; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Psd; mouse.
DR PRO; PR:Q5DTT2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q5DTT2; protein.
DR Bgee; ENSMUSG00000037126; Expressed in embryonic brain and 134 other tissues.
DR ExpressionAtlas; Q5DTT2; baseline and differential.
DR Genevisible; Q5DTT2; MM.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:SynGO-UCL.
DR GO; GO:0098999; C:extrinsic component of postsynaptic endosome membrane; IDA:SynGO-UCL.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO-UCL.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0031175; P:neuron projection development; IDA:SynGO-UCL.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF01369; Sec7; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Cell membrane;
KW Cell projection; Coiled coil; Guanine-nucleotide releasing factor;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1024
FT /note="PH and SEC7 domain-containing protein 1"
FT /id="PRO_0000334161"
FT DOMAIN 512..706
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 756..869
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 67..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 898..924
FT /evidence="ECO:0000255"
FT COILED 956..983
FT /evidence="ECO:0000255"
FT COMPBIAS 69..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..631
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:19494129"
FT /id="VSP_033637"
FT VAR_SEQ 518
FT /note="S -> SS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:19494129"
FT /id="VSP_041569"
FT VAR_SEQ 632..697
FT /note="FSQRYFQCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLE
FT GLNDGGDFPRELLK -> MIGVNSIHSSAGRLRSRSLCSVRYGRTHRGAETLCYGWPQR
FT SRSLKPVLYTDLVVSRLQSRKKKKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:19494129"
FT /id="VSP_033638"
FT MUTAGEN 621
FT /note="E->K: Significantly impaired guanine nucleotide
FT exchange factor activity on ARF6 in PC12 cells."
FT /evidence="ECO:0000269|PubMed:19494129"
SQ SEQUENCE 1024 AA; 109687 MW; 207A889E6D16CC99 CRC64;
MAQGAMRFCS EGDCAISPPR CPRRWLPEGP VPQSPPASMY GSTGSLIRRV VGPGPRGRDL
GRVTAPCTPL RAPPSPHIAP SPWGPSSPTG QPPPGAQSSV VIFRFVEKAS VRPLNGLPAS
GGLSRSWDLG GISAPRPTPA LGPGCNRKLR LEASTSDPLP AGGGSVLPGS RDPSRGPLVP
PQIGADGLYS SLPNGLGGTP EHLAMHFRGP ADTGFLNQGD TWSSPREVSS HAQRIARAKW
EFFYGSLDAP SSGAKPPEQV LPSRGVGSKQ GSGVAVGRAA KYSETDLDKV PLRCYRETDI
DEVLAEREEA DSAIESQPSS EGPHGTAQPP ASRPSPCPGP SSSLGSGNED DEAGGEEDVD
DEVFEASEGA RPGDHMPHSG LLKSPVPFLL GTSPSADGPD SFSCVFEAIL ESHRAKGTSY
SSLASLEALA SPGPTQSPFF TFEMPPQPPA PRPDPPAPAP LAPLEPDSGT SSAADGPWTQ
RREVEESDAG ATLAPRKELP SPSHSEDSFG LGAAPLGSEP PLSQLVSDSD SELDSTERLA
LGSTDTLSNG QKADLEAAQR LAKRLYRLDG FRKADVARHL GKNNDFSKLV AGEYLKFFVF
TGMTLDQALR VFLKELALMG ETQERERVLA HFSQRYFQCN PEALSSEDGA HTLTCALMLL
NTDLHGHNIG KRMTCGDFIG NLEGLNDGGD FPRELLKALY SSIKNEKLQW AIDEEELRRS
LSELADPNPK VIKRVSGGSG SSSSPFLDLT PEPGAAVYKH GALVRKVHAD PDCRKTPRGK
RGWKSFHGIL KGMILYLQKE EYQPGKALSE AELKNAISIH HALATRASDY SKRPHVFYLR
TADWRVFLFQ APSLEQMQSW ITRINVVAAM FSAPPFPAAV SSQKKFSRPL LPSAATRLSQ
EEQVRTHEAK LKAMASELRE HRAAHLGKKA RGKEADEQRQ KEAYLEFEKS RYGTYAALLR
VKMKAASEEL DTIEAALAQA GSTEDGCPPP HSSPSLRPKP TSQPRAQRPG SETRAGAGST
RPKP
