RHG22_HUMAN
ID RHG22_HUMAN Reviewed; 698 AA.
AC Q7Z5H3; A0AVP7; A5YM75; B4DED8; B9EGA0; C9JDM2; O00152; Q6ZSB0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Rho GTPase-activating protein 22;
DE AltName: Full=Rho-type GTPase-activating protein 22;
GN Name=ARHGAP22; Synonyms=RHOGAP2;
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 [MRNA] (ISOFORM 1).
RA Huang C.Q., Shan Y.X., Liu S.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Cerebellum, and Erythroleukemia;
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 4).
RC TISSUE=Brain;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung, and Testis;
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 [8]
RP IDENTIFICATION.
RX PubMed=15254788;
RA Katoh M., Katoh M.;
RT "Identification and characterization of ARHGAP24 and ARHGAP25 genes in
RT silico.";
RL Int. J. Mol. Med. 14:333-338(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359 AND SER-395, 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).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC transduction pathway that regulates endothelial cell capillary tube
CC formation during angiogenesis. Acts as a GTPase activator for the RAC1
CC by converting it to an inactive GDP-bound state. Inhibits RAC1-
CC dependent lamellipodia formation. May also play a role in transcription
CC regulation via its interaction with VEZF1, by regulating activity of
CC the endothelin-1 (EDN1) promoter (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VEZF1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q7Z5H3; O00555: CACNA1A; NbExp=2; IntAct=EBI-3866859, EBI-766279;
CC Q7Z5H3; O95273: CCNDBP1; NbExp=3; IntAct=EBI-3866859, EBI-748961;
CC Q7Z5H3-2; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-12084490, EBI-745369;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Mainly cytoplasmic. Some fraction is nuclear (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7Z5H3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5H3-2; Sequence=VSP_023705;
CC Name=3;
CC IsoId=Q7Z5H3-3; Sequence=VSP_023704;
CC Name=4;
CC IsoId=Q7Z5H3-4; Sequence=VSP_023703;
CC Name=5;
CC IsoId=Q7Z5H3-5; Sequence=VSP_053502;
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DR EMBL; AY324801; AAP85632.1; -; mRNA.
DR EMBL; AK127586; BAC87044.1; -; mRNA.
DR EMBL; AK293579; BAG57049.1; -; mRNA.
DR EMBL; U90908; AAB51057.1; -; mRNA.
DR EMBL; EF560749; ABQ59059.1; -; mRNA.
DR EMBL; AC016397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471187; EAW93127.1; -; Genomic_DNA.
DR EMBL; BC126444; AAI26445.1; -; mRNA.
DR EMBL; BC136319; AAI36320.1; -; mRNA.
DR CCDS; CCDS58079.1; -. [Q7Z5H3-3]
DR CCDS; CCDS58080.1; -. [Q7Z5H3-2]
DR CCDS; CCDS58081.1; -. [Q7Z5H3-5]
DR CCDS; CCDS7227.1; -. [Q7Z5H3-1]
DR RefSeq; NP_001242953.1; NM_001256024.1. [Q7Z5H3-2]
DR RefSeq; NP_001242954.1; NM_001256025.2. [Q7Z5H3-5]
DR RefSeq; NP_001242955.1; NM_001256026.1. [Q7Z5H3-3]
DR RefSeq; NP_001334667.1; NM_001347738.1. [Q7Z5H3-5]
DR RefSeq; NP_067049.2; NM_021226.3. [Q7Z5H3-1]
DR RefSeq; XP_011538306.1; XM_011540004.1.
DR AlphaFoldDB; Q7Z5H3; -.
DR SASBDB; Q7Z5H3; -.
DR SMR; Q7Z5H3; -.
DR BioGRID; 121832; 69.
DR IntAct; Q7Z5H3; 45.
DR MINT; Q7Z5H3; -.
DR STRING; 9606.ENSP00000412461; -.
DR iPTMnet; Q7Z5H3; -.
DR PhosphoSitePlus; Q7Z5H3; -.
DR BioMuta; ARHGAP22; -.
DR DMDM; 74750129; -.
DR EPD; Q7Z5H3; -.
DR jPOST; Q7Z5H3; -.
DR MassIVE; Q7Z5H3; -.
DR MaxQB; Q7Z5H3; -.
DR PaxDb; Q7Z5H3; -.
DR PeptideAtlas; Q7Z5H3; -.
DR PRIDE; Q7Z5H3; -.
DR ProteomicsDB; 3948; -.
DR ProteomicsDB; 69289; -. [Q7Z5H3-1]
DR ProteomicsDB; 69290; -. [Q7Z5H3-2]
DR ProteomicsDB; 69291; -. [Q7Z5H3-3]
DR ProteomicsDB; 69292; -. [Q7Z5H3-4]
DR Antibodypedia; 58456; 156 antibodies from 26 providers.
DR DNASU; 58504; -.
DR Ensembl; ENST00000249601.9; ENSP00000249601.4; ENSG00000128805.15. [Q7Z5H3-1]
DR Ensembl; ENST00000417247.6; ENSP00000410054.2; ENSG00000128805.15. [Q7Z5H3-3]
DR Ensembl; ENST00000417912.6; ENSP00000412461.2; ENSG00000128805.15. [Q7Z5H3-2]
DR Ensembl; ENST00000435790.6; ENSP00000416701.2; ENSG00000128805.15. [Q7Z5H3-5]
DR GeneID; 58504; -.
DR KEGG; hsa:58504; -.
DR MANE-Select; ENST00000249601.9; ENSP00000249601.4; NM_021226.4; NP_067049.2.
DR UCSC; uc001jgs.5; human. [Q7Z5H3-1]
DR CTD; 58504; -.
DR DisGeNET; 58504; -.
DR GeneCards; ARHGAP22; -.
DR HGNC; HGNC:30320; ARHGAP22.
DR HPA; ENSG00000128805; Tissue enhanced (brain).
DR MIM; 610585; gene.
DR neXtProt; NX_Q7Z5H3; -.
DR OpenTargets; ENSG00000128805; -.
DR PharmGKB; PA134979724; -.
DR VEuPathDB; HostDB:ENSG00000128805; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00950000183015; -.
DR HOGENOM; CLU_020795_0_0_1; -.
DR InParanoid; Q7Z5H3; -.
DR OMA; NEDLACS; -.
DR OrthoDB; 917149at2759; -.
DR PhylomeDB; Q7Z5H3; -.
DR TreeFam; TF323577; -.
DR PathwayCommons; Q7Z5H3; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q7Z5H3; -.
DR SIGNOR; Q7Z5H3; -.
DR BioGRID-ORCS; 58504; 12 hits in 1081 CRISPR screens.
DR ChiTaRS; ARHGAP22; human.
DR GenomeRNAi; 58504; -.
DR Pharos; Q7Z5H3; Tbio.
DR PRO; PR:Q7Z5H3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q7Z5H3; protein.
DR Bgee; ENSG00000128805; Expressed in C1 segment of cervical spinal cord and 115 other tissues.
DR ExpressionAtlas; Q7Z5H3; baseline and differential.
DR Genevisible; Q7Z5H3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; GTPase activation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..698
FT /note="Rho GTPase-activating protein 22"
FT /id="PRO_0000280469"
FT DOMAIN 37..145
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 155..349
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..687
FT /evidence="ECO:0000255"
FT COMPBIAS 420..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..329
FT /note="MLSPKIRQARRARSKSLVMGEQSRSPGRMPCPHRLGPVLKAGWLKKQRSIMK
FT NWQQRWFVLRGDQLFYYKDKDEIKPQGFISLQGTQVTELPPGPEDPGKHLFEISPGGAG
FT EREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGGIFGQRLEETVHHERKYGPR
FT LAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVAS
FT LLKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYIC
FT KFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIME -> MGQPREFWHLRSQV
FT PVPTCHLLTVQPWCLLPHPTPAGGRERRHSASSLLAALCLRKAVLRPHPAVLPGVGGCV
FT VLSSGRMKAPLRGGLALGTGPAPTKLQLLHDWQSEPGPSGWQQGPSPPLFPA (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_023703"
FT VAR_SEQ 1..107
FT /note="MLSPKIRQARRARSKSLVMGEQSRSPGRMPCPHRLGPVLKAGWLKKQRSIMK
FT NWQQRWFVLRGDQLFYYKDKDEIKPQGFISLQGTQVTELPPGPEDPGKHLFEISP ->
FT MPFWPIRCLKRSRRMPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023704"
FT VAR_SEQ 1..12
FT /note="MLSPKIRQARRA -> MLPTASSKRRTFAARYFT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053502"
FT VAR_SEQ 150
FT /note="G -> GGTARRSHAHPLEPLPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023705"
FT VARIANT 410
FT /note="T -> K (in dbSNP:rs1867586)"
FT /id="VAR_031153"
FT VARIANT 612
FT /note="R -> C (in dbSNP:rs3747853)"
FT /id="VAR_031154"
SQ SEQUENCE 698 AA; 76779 MW; 3CE8CEB0A9E5D0F8 CRC64;
MLSPKIRQAR RARSKSLVMG EQSRSPGRMP CPHRLGPVLK AGWLKKQRSI MKNWQQRWFV
LRGDQLFYYK DKDEIKPQGF ISLQGTQVTE LPPGPEDPGK HLFEISPGGA GEREKVPANP
EALLLMASSQ RDMEDWVQAI RRVIWAPLGG GIFGQRLEET VHHERKYGPR LAPLLVEQCV
DFIRERGLTE EGLFRMPGQA NLVRDLQDSF DCGEKPLFDS TTDVHTVASL LKLYLRELPE
PVVPFARYED FLSCAQLLTK DEGEGTLELA KQVSNLPQAN YNLLRYICKF LDEVQAYSNV
NKMSVQNLAT VFGPNILRPQ VEDPVTIMEG TSLVQHLMTV LIRKHSQLFT APVPEGPTSP
RGGLQCAVGW GSEEVTRDSQ GEPGGPGLPA HRTSSLDGAA VAVLSRTAPT GPGSRCSPGK
KVQTLPSWKS SFRQPRSLSG SPKGGGSSLE VPIISSGGNW LMNGLSSLRG HRRASSGDRL
KDSGSVQRLS TYDNVPAPGL VPGIPSVASM AWSGASSSES SVGGSLSSCT ACRASDSSAR
SSLHTDWALE PSPLPSSSED PKSLDLDHSM DEAGAGASNS EPSEPDSPTR EHARRSEALQ
GLVTELRAEL CRQRTEYERS VKRIEEGSAD LRKRMSRLEE ELDQEKKKYI MLEIKLRNSE
RAREDAERRN QLLQREMEEF FSTLGSLTVG AKGARAPK
