RHG33_HUMAN
ID RHG33_HUMAN Reviewed; 1287 AA.
AC O14559; O14552; O14560; Q6ZSP6; Q96CP3; Q9NT23;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Rho GTPase-activating protein 33;
DE AltName: Full=Rho-type GTPase-activating protein 33;
DE AltName: Full=Sorting nexin-26;
DE AltName: Full=Tc10/CDC42 GTPase-activating protein;
GN Name=ARHGAP33; Synonyms=SNX26, TCGAP;
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 4).
RA Hong W.;
RT "A novel member (SNX26) of the sorting nexin family.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Hippocampus;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 426-1287.
RC TISSUE=Testis;
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 MRNA] OF 993-1287.
RC TISSUE=Pancreas;
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 INTERACTION WITH NEK6.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Could play an important role in the regulation of glucose
CC transport by insulin. May act as a downstream effector of RHOQ/TC10 in
CC the regulation of insulin-stimulated glucose transport (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Specifically interacts with CDC42 and RHOQ/TC10 through its
CC Rho-GAP domain (By similarity). Interacts with NEK6. {ECO:0000250,
CC ECO:0000269|PubMed:20873783}.
CC -!- INTERACTION:
CC O14559; P06241: FYN; NbExp=2; IntAct=EBI-1210010, EBI-515315;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O14559-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14559-10; Sequence=VSP_014287, VSP_014292;
CC Name=3;
CC IsoId=O14559-11; Sequence=VSP_014291;
CC Name=4;
CC IsoId=O14559-12; Sequence=VSP_014288, VSP_014289, VSP_014290;
CC -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB81198.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=BAC86902.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY044864; AAK97795.1; -; mRNA.
DR EMBL; AK096338; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK127255; BAC86902.1; ALT_FRAME; mRNA.
DR EMBL; AC002398; AAB81197.1; -; Genomic_DNA.
DR EMBL; AC002398; AAB81198.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL137579; CAB70821.1; -; mRNA.
DR EMBL; BC014084; AAH14084.2; -; mRNA.
DR CCDS; CCDS12477.1; -. [O14559-11]
DR CCDS; CCDS54254.1; -. [O14559-10]
DR PIR; T00704; T00704.
DR PIR; T00705; T00705.
DR PIR; T46289; T46289.
DR RefSeq; NP_001166101.1; NM_001172630.1. [O14559-10]
DR RefSeq; NP_443180.2; NM_052948.3. [O14559-11]
DR RefSeq; XP_005258545.1; XM_005258488.1.
DR RefSeq; XP_011524721.1; XM_011526419.1.
DR AlphaFoldDB; O14559; -.
DR SMR; O14559; -.
DR BioGRID; 125448; 5.
DR IntAct; O14559; 3.
DR GlyGen; O14559; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O14559; -.
DR PhosphoSitePlus; O14559; -.
DR BioMuta; ARHGAP33; -.
DR EPD; O14559; -.
DR jPOST; O14559; -.
DR MassIVE; O14559; -.
DR MaxQB; O14559; -.
DR PaxDb; O14559; -.
DR PeptideAtlas; O14559; -.
DR PRIDE; O14559; -.
DR ProteomicsDB; 48084; -. [O14559-1]
DR ProteomicsDB; 48085; -. [O14559-10]
DR ProteomicsDB; 48086; -. [O14559-11]
DR ProteomicsDB; 48087; -. [O14559-12]
DR Antibodypedia; 29527; 134 antibodies from 26 providers.
DR DNASU; 115703; -.
DR Ensembl; ENST00000007510.9; ENSP00000007510.6; ENSG00000004777.19. [O14559-1]
DR Ensembl; ENST00000314737.9; ENSP00000320038.4; ENSG00000004777.19. [O14559-11]
DR Ensembl; ENST00000378944.9; ENSP00000368227.5; ENSG00000004777.19. [O14559-10]
DR GeneID; 115703; -.
DR KEGG; hsa:115703; -.
DR MANE-Select; ENST00000007510.9; ENSP00000007510.6; NM_001366178.1; NP_001353107.1.
DR UCSC; uc002obs.3; human. [O14559-1]
DR CTD; 115703; -.
DR DisGeNET; 115703; -.
DR GeneCards; ARHGAP33; -.
DR HGNC; HGNC:23085; ARHGAP33.
DR HPA; ENSG00000004777; Low tissue specificity.
DR MIM; 614902; gene.
DR neXtProt; NX_O14559; -.
DR OpenTargets; ENSG00000004777; -.
DR PharmGKB; PA165393003; -.
DR VEuPathDB; HostDB:ENSG00000004777; -.
DR eggNOG; KOG1449; Eukaryota.
DR GeneTree; ENSGT00940000155110; -.
DR InParanoid; O14559; -.
DR OMA; NTSMHIR; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; O14559; -.
DR TreeFam; TF351451; -.
DR PathwayCommons; O14559; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR SignaLink; O14559; -.
DR SIGNOR; O14559; -.
DR BioGRID-ORCS; 115703; 19 hits in 1081 CRISPR screens.
DR ChiTaRS; ARHGAP33; human.
DR GeneWiki; SNX26; -.
DR GenomeRNAi; 115703; -.
DR Pharos; O14559; Tbio.
DR PRO; PR:O14559; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14559; protein.
DR Bgee; ENSG00000004777; Expressed in cortical plate and 154 other tissues.
DR ExpressionAtlas; O14559; baseline and differential.
DR Genevisible; O14559; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR035510; ARHGAP33.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15729:SF11; PTHR15729:SF11; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Methylation; Phosphoprotein;
KW Protein transport; Reference proteome; SH3 domain; Transport.
FT CHAIN 1..1287
FT /note="Rho GTPase-activating protein 33"
FT /id="PRO_0000056721"
FT DOMAIN 59..168
FT /note="PX; atypical"
FT DOMAIN 186..248
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 315..510
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..897
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1072
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YF9"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YF9"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YF9"
FT MOD_RES 1169
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80YF9"
FT MOD_RES 1244
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q80YF9"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014287"
FT VAR_SEQ 1..2
FT /note="MV -> MLSLSLCSHLWGPLILSALQ (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014288"
FT VAR_SEQ 168..228
FT /note="LDNHGRRLLLSEEASLNIPAVAAAHVIKRYTAQAPDELSFEVGDIVSVIDMP
FT PTEDRSWWR -> VGLGRGLGDSEWVRGCVCHHAQHREILDGNRVASAVEDEGAEVDGE
FT AFRWGSLWVGESWDM (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014289"
FT VAR_SEQ 229..1287
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014290"
FT VAR_SEQ 648..808
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014291"
FT VAR_SEQ 998..1025
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014292"
FT CONFLICT 119
FT /note="F -> S (in Ref. 2; AK096338)"
FT /evidence="ECO:0000305"
FT CONFLICT 1100
FT /note="P -> L (in Ref. 4; CAB70821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1287 AA; 137213 MW; 802900F18B640DC0 CRC64;
MVARSTDSLD GPGEGSVQPL PTAGGPSVKG KPGKRLSAPR GPFPRLADCA HFHYENVDFG
HIQLLLSPDR EGPSLSGENE LVFGVQVTCQ GRSWPVLRSY DDFRSLDAHL HRCIFDRRFS
CLPELPPPPE GARAAQMLVP LLLQYLETLS GLVDSNLNCG PVLTWMELDN HGRRLLLSEE
ASLNIPAVAA AHVIKRYTAQ APDELSFEVG DIVSVIDMPP TEDRSWWRGK RGFQVGFFPS
ECVELFTERP GPGLKADADG PPCGIPAPQG ISSLTSAVPR PRGKLAGLLR TFMRSRPSRQ
RLRQRGILRQ RVFGCDLGEH LSNSGQDVPQ VLRCCSEFIE AHGVVDGIYR LSGVSSNIQR
LRHEFDSERI PELSGPAFLQ DIHSVSSLCK LYFRELPNPL LTYQLYGKFS EAMSVPGEEE
RLVRVHDVIQ QLPPPHYRTL EYLLRHLARM ARHSANTSMH ARNLAIVWAP NLLRSMELES
VGMGGAAAFR EVRVQSVVVE FLLTHVDVLF SDTFTSAGLD PAGRCLLPRP KSLAGSCPST
RLLTLEEAQA RTQGRLGTPT EPTTPKAPAS PAERRKGERG EKQRKPGGSS WKTFFALGRG
PSVPRKKPLP WLGGTRAPPQ PSGSRPDTVT LRSAKSEESL SSQASGAGLQ RLHRLRRPHS
SSDAFPVGPA PAGSCESLSS SSSSESSSSE SSSSSSESSA AGLGALSGSP SHRTSAWLDD
GDELDFSPPR CLEGLRGLDF DPLTFRCSSP TPGDPAPPAS PAPPAPASAF PPRVTPQAIS
PRGPTSPASP AALDISEPLA VSVPPAVLEL LGAGGAPASA TPTPALSPGR SLRPHLIPLL
LRGAEAPLTD ACQQEMCSKL RGAQGPLGPD MESPLPPPPL SLLRPGGAPP PPPKNPARLM
ALALAERAQQ VAEQQSQQEC GGTPPASQSP FHRSLSLEVG GEPLGTSGSG PPPNSLAHPG
AWVPGPPPYL PRQQSDGSLL RSQRPMGTSR RGLRGPAQVS AQLRAGGGGR DAPEAAAQSP
CSVPSQVPTP GFFSPAPREC LPPFLGVPKP GLYPLGPPSF QPSSPAPVWR SSLGPPAPLD
RGENLYYEIG ASEGSPYSGP TRSWSPFRSM PPDRLNASYG MLGQSPPLHR SPDFLLSYPP
APSCFPPDHL GYSAPQHPAR RPTPPEPLYV NLALGPRGPS PASSSSSSPP AHPRSRSDPG
PPVPRLPQKQ RAPWGPRTPH RVPGPWGPPE PLLLYRAAPP AYGRGGELHR GSLYRNGGQR
GEGAGPPPPY PTPSWSLHSE GQTRSYC
