RGPA2_MOUSE
ID RGPA2_MOUSE Reviewed; 1872 AA.
AC A3KGS3; A3KGS5; B7ZCU9; Q3TZD9; Q4VA60; Q69ZM8; Q7TQL4; Q8BYP2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ral GTPase-activating protein subunit alpha-2;
DE AltName: Full=250 kDa substrate of Akt;
DE Short=AS250;
DE AltName: Full=P220;
GN Name=Ralgapa2; Synonyms=Kiaa1272;
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 RALGAPB, AND
RP TISSUE SPECIFICITY.
RX PubMed=16490346; DOI=10.1016/j.cellsig.2006.01.002;
RA Gridley S., Chavez J.A., Lane W.S., Lienhard G.E.;
RT "Adipocytes contain a novel complex similar to the tuberous sclerosis
RT complex.";
RL Cell. Signal. 18:1626-1632(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 MRNA] OF 1-734 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Inner ear;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 975-1872 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1196-1872 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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 1406-1872 (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819 AND SER-820, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-376; SER-379;
RP SER-486; SER-819 AND SER-820, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Catalytic subunit of the heterodimeric RalGAP2 complex which
CC acts as a GTPase activator for the Ras-like small GTPases RALA and
CC RALB. {ECO:0000250}.
CC -!- SUBUNIT: Component of the heterodimeric RalGAP2 complex with RALGAPB.
CC Heterodimerization is required for activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A3KGS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3KGS3-2; Sequence=VSP_025251, VSP_025252;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in testis, pancreas, lung,
CC thymus, brown fat, and white fat. {ECO:0000269|PubMed:16490346}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30146.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC30146.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to erroneous C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM46007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM46125.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM46200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL845273; CAM46125.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845430; CAM46125.1; JOINED; Genomic_DNA.
DR EMBL; AL935056; CAM46125.1; JOINED; Genomic_DNA.
DR EMBL; AL845273; CAX15311.1; -; Genomic_DNA.
DR EMBL; AL845430; CAX15311.1; JOINED; Genomic_DNA.
DR EMBL; AL935056; CAX15311.1; JOINED; Genomic_DNA.
DR EMBL; AL845430; CAM46200.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845273; CAM46200.1; JOINED; Genomic_DNA.
DR EMBL; AL935056; CAM46200.1; JOINED; Genomic_DNA.
DR EMBL; AL845430; CAX15398.1; -; Genomic_DNA.
DR EMBL; AL845273; CAX15398.1; JOINED; Genomic_DNA.
DR EMBL; AL935056; CAX15398.1; JOINED; Genomic_DNA.
DR EMBL; AL935056; CAM46007.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845273; CAM46007.1; JOINED; Genomic_DNA.
DR EMBL; AL845430; CAM46007.1; JOINED; Genomic_DNA.
DR EMBL; AL935056; CAX15696.1; -; Genomic_DNA.
DR EMBL; AL845273; CAX15696.1; JOINED; Genomic_DNA.
DR EMBL; AL845430; CAX15696.1; JOINED; Genomic_DNA.
DR EMBL; AK038838; BAC30146.1; ALT_SEQ; mRNA.
DR EMBL; AK157932; BAE34270.1; -; mRNA.
DR EMBL; BC053994; AAH53994.1; -; mRNA.
DR EMBL; BC096528; AAH96528.1; -; mRNA.
DR EMBL; AK173140; BAD32418.1; -; mRNA.
DR RefSeq; NP_001028520.2; NM_001033348.3.
DR AlphaFoldDB; A3KGS3; -.
DR SMR; A3KGS3; -.
DR BioGRID; 232342; 12.
DR STRING; 10090.ENSMUSP00000105613; -.
DR iPTMnet; A3KGS3; -.
DR PhosphoSitePlus; A3KGS3; -.
DR EPD; A3KGS3; -.
DR jPOST; A3KGS3; -.
DR MaxQB; A3KGS3; -.
DR PaxDb; A3KGS3; -.
DR PeptideAtlas; A3KGS3; -.
DR PRIDE; A3KGS3; -.
DR ProteomicsDB; 253259; -. [A3KGS3-1]
DR ProteomicsDB; 253260; -. [A3KGS3-2]
DR Antibodypedia; 59154; 55 antibodies from 16 providers.
DR DNASU; 241694; -.
DR Ensembl; ENSMUST00000131824; ENSMUSP00000122039; ENSMUSG00000037110. [A3KGS3-1]
DR GeneID; 241694; -.
DR KEGG; mmu:241694; -.
DR CTD; 57186; -.
DR MGI; MGI:3036245; Ralgapa2.
DR VEuPathDB; HostDB:ENSMUSG00000037110; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00950000183139; -.
DR HOGENOM; CLU_001676_0_0_1; -.
DR InParanoid; A3KGS3; -.
DR OrthoDB; 157372at2759; -.
DR PhylomeDB; A3KGS3; -.
DR TreeFam; TF324484; -.
DR BioGRID-ORCS; 241694; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ralgapa2; mouse.
DR PRO; PR:A3KGS3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A3KGS3; protein.
DR Bgee; ENSMUSG00000037110; Expressed in ear vesicle and 215 other tissues.
DR ExpressionAtlas; A3KGS3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IGI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IGI:MGI.
DR GO; GO:0032484; P:Ral protein signal transduction; IMP:MGI.
DR GO; GO:0060178; P:regulation of exocyst localization; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR027107; Tuberin/Ral-act_asu.
DR PANTHER; PTHR10063; PTHR10063; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1872
FT /note="Ral GTPase-activating protein subunit alpha-2"
FT /id="PRO_0000286973"
FT DOMAIN 1634..1842
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 350..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 696
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:Q2PPJ7"
FT MOD_RES 715
FT /note="Phosphothreonine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:Q2PPJ7"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PPJ7"
FT VAR_SEQ 1789..1807
FT /note="VPFFGPLFDGAIVSGKLLP -> LLLKIEKFHSLGPCSMERS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025251"
FT VAR_SEQ 1808..1872
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025252"
FT CONFLICT 436
FT /note="Q -> R (in Ref. 2; BAC30146)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="K -> E (in Ref. 2; BAE34270)"
FT /evidence="ECO:0000305"
FT CONFLICT 1511
FT /note="N -> H (in Ref. 4; AAH53994)"
FT /evidence="ECO:0000305"
FT CONFLICT 1727
FT /note="D -> V (in Ref. 5; BAD32418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1872 AA; 210288 MW; CCB0AA23790D863A CRC64;
MFSRRSHGDV KKSTQKVLDP KKDVLTRLKH LRALLDNVDA SDLKQFFETN YSQIYFIFYE
NFITLENSLK LKGNNKSQRE ELDSILFLFE KILQFLPERI FFRWHYQSIG STLKKLLHTG
NSIKIRCEGI RLFLLWLQAL QTNCAEEQVL IFACLVPGFP AVLSSRGPCT LETLINPSPS
IVDAKIYPEE ITPLLPAISG EKIAEDQTCF FLQILLKYMV IQAASLEWKN KENQDTGFKF
LFTLFRKYYL PHLFPSFTKL TNIYKPVLEI PHLRPKPVYV TVTRDNETIY STKIPYMAAR
VVFIKWIVTF FLEKKYLTAT QNTKNGVDVL PKIIQTVGGG AIQEKVPELD GAGSTEQDKS
HSNSSTLSDR RLSNSSLCSI EEEHRTVYEM VQRILLSTRG YVNFVNEVFR QAFLLPSCEI
SVTRKVVQVY RKWILQNKPV FMEEPDKKDV AQEDADKLGL SETDSKEASS ESSGHKRSSS
WGRTYSFTSA MSRGCVTEED NTNVKAGAQA MLQVFLTNAA NVFLLEPCAE VPMLLREQVD
ASKAVLIIFR RMIMELTMNQ KTWEQMLQIL LRITEAVMQK PKDKHVKDLF AQSLAGLLFR
TLIVAWIRAN LCVYISRELW DDFLRVLSSL TEWEELITEW SNIMDSLTAV LARTVYGVEM
TNLPLDKLSE QKEKKQRGKG CILEPQKGTA VGRSFSLSWR SHPDVTEPMR FRSATTSGAP
GVEKARNTVR QKATEVEEFQ QAESTAAADC DYLVVGQQQV PRSSSTSDIT ERLYSDSSQG
QKVEHSQNLS SSEPKSVQES KGHVTHEHEG ITMLVRRSSS PAELELKDDL QQAHGRCRQR
QTSESTGSDT VVGYSNEAEL PVSPWQACEE DPDLSTPTDA VADSDARHWL QLSPTDASNL
TDSRECLADD CSIIAGGNLT GWHPDSAAVL WRRVLGILGD VNNIQSPKIH AKVFGYLYEL
WYKLAKIRDN LAISLDNQSS PSPPLLIPPL RMFASWLFKA TTLPNEYKEG KLQAYKLICA
MMTRRQDVLP NSDFLVHFYL VMHLGLTSED QDVLNTIIKN CSPRFFSLGL PGFSMLVGDF
ITAAARVLST DMLAAPRSEA LTLLGSLVCF PNTYQEIPLL QSVPEVSDVV TGAEDVKHYL
INILLKNATE EPNECARCIA ICSLGVWICE ELAQSASHPQ VKDAINVIGV TLKFPNKIVA
QVACDVLQLL VSYWEKLQMF ETALPRKMAE ILVATIAFLL PSAEYSSVET DKKFIVSLLL
CLLDWCMALP VSALLHPVST AVLEELHPSR APLLDYIYRV LHCCVCGSST YTQQSHYTLT
LADLSSTDYD PFLPLANVRN SEPIQYHSSA DLGNLLTVEE EKKRRSVELI PLTARMVMAH
LVNHLGHYPL SGGPAVLHSL VSENHDNAHV EGTELSSEVF RSPNLQLFVF NDSTLISYLQ
TPAEGPAGGT SGGSLSDVRV IVRDISGKYS WDGKVLYGPL EGRLAPNGRN PSFQISGWHH
HTCGPQKDLF NGEEGDDVLD KLLENIGHTS PECLLPSQLN LNEPSPTPCA MNWDQEKAIM
EVILRQSAQE DEYVQRCNSD SSVTVTSQGQ PSPVEPRGPF YFCRLLLDDL GMNSWDRRKN
FHLLKKNSKL LRELKNLDSR QCRETHKIAV FYIAEGQEDK CSILANERGS QAYEDFVAGL
GWEVDLSTHC GFMGGLQRNG STGQTAPYYA TSTVEVIFHV STRMPSDSDD SLTKKLRHLG
NDEVHIVWSE HSRDYRRGII PTAFGDVSII IYPMKNHMFF ITITKKPEVP FFGPLFDGAI
VSGKLLPSLI CATCINASRA VKCLIPLYQS FYEERALYLE AIIQNHREVM TFEDFAAQVF
SPSPSYSVSG TD
