RHG44_HUMAN
ID RHG44_HUMAN Reviewed; 818 AA.
AC Q17R89; A6NCP5; A8MQB2; O75160; Q7Z5Z7; Q9Y4Q4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Rho GTPase-activating protein 44 {ECO:0000305};
DE AltName: Full=NPC-A-10;
DE AltName: Full=Rho-type GTPase-activating protein RICH2;
DE AltName: Full=RhoGAP interacting with CIP4 homologs protein 2;
DE Short=RICH-2;
GN Name=ARHGAP44 {ECO:0000312|HGNC:HGNC:29096}; Synonyms=KIAA0672, RICH2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-508 (ISOFORM 1/2).
RC TISSUE=Nasopharyngeal carcinoma;
RA Shu J., Li G., He X.;
RT "Construction of cDNA expression library from nasopharyngeal carcinoma
RT tissue and screening of antigenic genes.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 356-758 (ISOFORM 2).
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 [7]
RP FUNCTION AS A GTPASE-ACTIVATING PROTEIN, AND TISSUE SPECIFICITY.
RX PubMed=11431473; DOI=10.1074/jbc.m103540200;
RA Richnau N., Aspenstroem P.;
RT "Rich, a rho GTPase-activating protein domain-containing protein involved
RT in signaling by Cdc42 and Rac1.";
RL J. Biol. Chem. 276:35060-35070(2001).
RN [8]
RP INTERACTION WITH BST2.
RX PubMed=19273615; DOI=10.1083/jcb.200804154;
RA Rollason R., Korolchuk V., Hamilton C., Jepson M., Banting G.;
RT "A CD317/tetherin-RICH2 complex plays a critical role in the organization
RT of the subapical actin cytoskeleton in polarized epithelial cells.";
RL J. Cell Biol. 184:721-736(2009).
CC -!- FUNCTION: GTPase-activating protein (GAP) that stimulates the GTPase
CC activity of Rho-type GTPases. Thereby, controls Rho-type GTPases
CC cycling between their active GTP-bound and inactive GDP-bound states.
CC Acts as a GAP at least for CDC42 and RAC1 (PubMed:11431473). In
CC neurons, is involved in dendritic spine formation and synaptic
CC plasticity in a specific RAC1-GAP activity (By similarity). Limits the
CC initiation of exploratory dendritic filopodia. Recruited to actin-
CC patches that seed filopodia, binds specifically to plasma membrane
CC sections that are deformed inward by acto-myosin mediated contractile
CC forces. Acts through GAP activity on RAC1 to reduce actin
CC polymerization necessary for filopodia formation (By similarity). In
CC association with SHANK3, promotes GRIA1 exocytosis from recycling
CC endosomes and spine morphological changes associated to long-term
CC potentiation (By similarity). {ECO:0000250|UniProtKB:F1LQX4,
CC ECO:0000250|UniProtKB:Q5SSM3, ECO:0000269|PubMed:11431473}.
CC -!- SUBUNIT: Interacts with BST2 (via cytoplasmic domain). Interacts
CC (probably via PDZ-binding motif) with SHANK3 (via PDZ domain); the
CC interaction takes place in dendritic spines and promotes GRIA1
CC exocytosis. {ECO:0000269|PubMed:19273615}.
CC -!- INTERACTION:
CC Q17R89-2; Q15642: TRIP10; NbExp=3; IntAct=EBI-10238335, EBI-739936;
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q5SSM3}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q5SSM3}. Presynapse
CC {ECO:0000250|UniProtKB:Q5SSM3}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:F1LQX4}. Note=In CA1 hippocampal synapses,
CC detected at both presynaptic and postsynaptic sites (By similarity).
CC Located in convoluted dendritic plasma membrane sections enriched in
CC polymerized actin and myosin (patches) along dendrites where often
CC emerge filopodia (By similarity). {ECO:0000250|UniProtKB:F1LQX4,
CC ECO:0000250|UniProtKB:Q5SSM3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q17R89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q17R89-2; Sequence=VSP_053616, VSP_053617, VSP_053618;
CC Name=3;
CC IsoId=Q17R89-3; Sequence=VSP_053616;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed at weak level
CC in other tissues. {ECO:0000269|PubMed:11431473}.
CC -!- DOMAIN: Rho-GAP domain is required to promote GRIA1 exocytosis from
CC recycling endosomes. Rho-GAP and BAR domains are necessary for the
CC control of long-term potentiation in hippocampal neurons (By
CC similarity). In dendrites, BAR domain mediates the recruitment to
CC patches where plasma membrane is deformed by acto-myosin mediated
CC contractile forces (By similarity). {ECO:0000250|UniProtKB:F1LQX4,
CC ECO:0000250|UniProtKB:Q5SSM3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP73805.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP73805.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA31647.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014572; BAA31647.2; ALT_INIT; mRNA.
DR EMBL; AK294538; BAG57745.1; -; mRNA.
DR EMBL; AC005274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117412; AAI17413.1; -; mRNA.
DR EMBL; BC117416; AAI17417.1; -; mRNA.
DR EMBL; BC143853; AAI43854.1; -; mRNA.
DR EMBL; AY320403; AAP73805.1; ALT_SEQ; mRNA.
DR EMBL; AL096728; CAB46376.1; -; mRNA.
DR CCDS; CCDS45616.1; -. [Q17R89-1]
DR CCDS; CCDS82077.1; -. [Q17R89-3]
DR PIR; A59433; A59433.
DR RefSeq; NP_001308095.1; NM_001321166.1. [Q17R89-3]
DR RefSeq; NP_001308097.1; NM_001321168.1.
DR RefSeq; NP_055674.4; NM_014859.5. [Q17R89-1]
DR AlphaFoldDB; Q17R89; -.
DR SMR; Q17R89; -.
DR BioGRID; 115241; 40.
DR IntAct; Q17R89; 16.
DR MINT; Q17R89; -.
DR STRING; 9606.ENSP00000368994; -.
DR iPTMnet; Q17R89; -.
DR PhosphoSitePlus; Q17R89; -.
DR SwissPalm; Q17R89; -.
DR BioMuta; ARHGAP44; -.
DR DMDM; 121948837; -.
DR EPD; Q17R89; -.
DR jPOST; Q17R89; -.
DR MassIVE; Q17R89; -.
DR MaxQB; Q17R89; -.
DR PaxDb; Q17R89; -.
DR PeptideAtlas; Q17R89; -.
DR PRIDE; Q17R89; -.
DR ProteomicsDB; 61137; -. [Q17R89-1]
DR ProteomicsDB; 849; -.
DR Antibodypedia; 47980; 108 antibodies from 21 providers.
DR DNASU; 9912; -.
DR Ensembl; ENST00000340825.7; ENSP00000342566.3; ENSG00000006740.18. [Q17R89-3]
DR Ensembl; ENST00000379672.10; ENSP00000368994.5; ENSG00000006740.18. [Q17R89-1]
DR GeneID; 9912; -.
DR KEGG; hsa:9912; -.
DR MANE-Select; ENST00000379672.10; ENSP00000368994.5; NM_014859.6; NP_055674.4.
DR UCSC; uc002gnr.5; human. [Q17R89-1]
DR CTD; 9912; -.
DR DisGeNET; 9912; -.
DR GeneCards; ARHGAP44; -.
DR HGNC; HGNC:29096; ARHGAP44.
DR HPA; ENSG00000006740; Tissue enhanced (brain).
DR MIM; 617716; gene.
DR neXtProt; NX_Q17R89; -.
DR OpenTargets; ENSG00000006740; -.
DR VEuPathDB; HostDB:ENSG00000006740; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000157296; -.
DR InParanoid; Q17R89; -.
DR OMA; THDEGNI; -.
DR OrthoDB; 821331at2759; -.
DR PhylomeDB; Q17R89; -.
DR TreeFam; TF316514; -.
DR PathwayCommons; Q17R89; -.
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; Q17R89; -.
DR SIGNOR; Q17R89; -.
DR BioGRID-ORCS; 9912; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; ARHGAP44; human.
DR GenomeRNAi; 9912; -.
DR Pharos; Q17R89; Tbio.
DR PRO; PR:Q17R89; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q17R89; protein.
DR Bgee; ENSG00000006740; Expressed in lateral nuclear group of thalamus and 173 other tissues.
DR ExpressionAtlas; Q17R89; baseline and differential.
DR Genevisible; Q17R89; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0031256; C:leading edge membrane; IDA:FlyBase.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0098886; P:modification of dendritic spine; IBA:GO_Central.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IBA:GO_Central.
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; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Endosome; Exocytosis;
KW GTPase activation; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..818
FT /note="Rho GTPase-activating protein 44"
FT /id="PRO_0000280480"
FT DOMAIN 14..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 255..445
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 467..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..818
FT /note="Interaction with BST2"
FT /evidence="ECO:0000269|PubMed:19273615"
FT REGION 789..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 815..818
FT /note="PDZ-binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 541..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..747
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSM3"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1LQX4"
FT VAR_SEQ 509..514
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_053616"
FT VAR_SEQ 773..774
FT /note="DL -> AV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_053617"
FT VAR_SEQ 775..818
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_053618"
FT VARIANT 463
FT /note="V -> M (in dbSNP:rs3213688)"
FT /id="VAR_031159"
FT CONFLICT 346
FT /note="E -> G (in Ref. 5; AAP73805)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="R -> M (in Ref. 6; CAB46376)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="P -> L (in Ref. 1; BAA31647)"
FT /evidence="ECO:0000305"
FT MOTIF Q17R89-2:764..767
FT /note="PDZ-binding"
SQ SEQUENCE 818 AA; 89247 MW; FCAC06CEDB522C09 CRC64;
MKKQFNRMRQ LANQTVGRAE KTEVLSEDLL QVEKRLELVK QVSHSTHKKL TACLQGQQGA
EADKRSKKLP LTTLAQCLME GSAILGDDTL LGKMLKLCGE TEDKLAQELI HFELQVERDV
IEPLFLLAEV EIPNIQKQRK HLAKLVLDMD SSRTRWQQTS KSSGLSSSLQ PAGAKADALR
EEMEEAANRV EICRDQLSAD MYSFVAKEID YANYFQTLIE VQAEYHRKSL TLLQAVLPQI
KAQQEAWVEK PSFGKPLEEH LTISGREIAF PIEACVTMLL ECGMQEEGLF RVAPSASKLK
KLKAALDCCV VDVQEYSADP HAIAGALKSY LRELPEPLMT FELYDEWIQA SNVQEQDKKL
QALWNACEKL PKANHNNIRY LIKFLSKLSE YQDVNKMTPS NMAIVLGPNL LWPQAEGNIT
EMMTTVSLQI VGIIEPIIQH ADWFFPGEIE FNITGNYGSP VHVNHNANYS SMPSPDMDPA
DRRQPEQARR PLSVATDNMM LEFYKKDGLR KIQSMGVRVM DTNWVARRGS SAGRKVSCAP
PSMQPPAPPA ELAAPLPSPL PEQPLDSPAA PALSPSGLGL QPGPERTSTT KSKELSPGSA
QKGSPGSSQG TACAGTQPGA QPGAQPGASP SPSQPPADQS PHTLRKVSKK LAPIPPKVPF
GQPGAMADQS AGQPSPVSLS PTPPSTPSPY GLSYPQGYSL ASGQLSPAAA PPLASPSVFT
STLSKSRPTP KPRQRPTLPP PQPPTVNLSA SSPQSTEAPM LDGMSPGESM STDLVHFDIP
SIHIELGSTL RLSPLEHMRR HSVTDKRDSE EESESTAL
