RHG19_HUMAN
ID RHG19_HUMAN Reviewed; 494 AA.
AC Q14CB8; A1XCP1; B4DZR1; Q14CF2; Q5J8M2; Q5T460; Q5T462; Q68DG6; Q8N9X1;
AC Q8NF34; Q8TEK1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Rho GTPase-activating protein 19;
DE AltName: Full=Rho-type GTPase-activating protein 19;
GN Name=ARHGAP19;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=17454002; DOI=10.1080/10425170600752965;
RA Lv L., Xu J., Zhao S., Chen C., Zhao X., Gu S., Ji C., Xie Y., Mao Y.;
RT "Sequence analysis of a human RhoGAP domain-containing gene and
RT characterization of its expression in human multiple tissues.";
RL DNA Seq. 18:184-189(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis;
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), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3-427 (ISOFORM 5).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
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] (ISOFORMS 1 AND 6).
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND THR-478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-422 AND SER-438, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- INTERACTION:
CC Q14CB8; P54252: ATXN3; NbExp=4; IntAct=EBI-954525, EBI-946046;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17454002}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q14CB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14CB8-2; Sequence=VSP_023701;
CC Name=3;
CC IsoId=Q14CB8-3; Sequence=VSP_023696;
CC Name=4;
CC IsoId=Q14CB8-4; Sequence=VSP_023695;
CC Name=5;
CC IsoId=Q14CB8-5; Sequence=VSP_023698, VSP_023699;
CC Name=6;
CC IsoId=Q14CB8-6; Sequence=VSP_023697;
CC Name=7;
CC IsoId=Q14CB8-7; Sequence=VSP_023700;
CC -!- TISSUE SPECIFICITY: Strong expression in fetal heart, brain, placenta,
CC lung, liver, skeletal muscle, kidney and pancreas. Weak expression in
CC adult pancreas, spleen, thymus, and ovary.
CC {ECO:0000269|PubMed:17454002}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC04165.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ338460; ABC69298.1; -; mRNA.
DR EMBL; AY336750; AAR02412.1; -; mRNA.
DR EMBL; AK093441; BAC04165.1; ALT_FRAME; mRNA.
DR EMBL; AK074122; BAB84948.1; ALT_INIT; mRNA.
DR EMBL; AK090447; BAC03428.1; -; mRNA.
DR EMBL; AK303055; BAG64173.1; -; mRNA.
DR EMBL; CR749412; CAH18254.1; -; mRNA.
DR EMBL; AL359385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49952.1; -; Genomic_DNA.
DR EMBL; BC113888; AAI13889.1; -; mRNA.
DR EMBL; BC114490; AAI14491.1; -; mRNA.
DR CCDS; CCDS58092.1; -. [Q14CB8-3]
DR CCDS; CCDS73175.1; -. [Q14CB8-6]
DR CCDS; CCDS7454.2; -. [Q14CB8-1]
DR RefSeq; NP_001191229.1; NM_001204300.1. [Q14CB8-6]
DR RefSeq; NP_001243352.1; NM_001256423.1. [Q14CB8-3]
DR RefSeq; NP_116289.4; NM_032900.5. [Q14CB8-1]
DR AlphaFoldDB; Q14CB8; -.
DR SMR; Q14CB8; -.
DR BioGRID; 124412; 58.
DR IntAct; Q14CB8; 35.
DR STRING; 9606.ENSP00000351333; -.
DR iPTMnet; Q14CB8; -.
DR MetOSite; Q14CB8; -.
DR PhosphoSitePlus; Q14CB8; -.
DR BioMuta; ARHGAP19; -.
DR DMDM; 121948181; -.
DR EPD; Q14CB8; -.
DR jPOST; Q14CB8; -.
DR MassIVE; Q14CB8; -.
DR MaxQB; Q14CB8; -.
DR PaxDb; Q14CB8; -.
DR PeptideAtlas; Q14CB8; -.
DR PRIDE; Q14CB8; -.
DR ProteomicsDB; 60317; -. [Q14CB8-1]
DR ProteomicsDB; 60318; -. [Q14CB8-2]
DR ProteomicsDB; 60319; -. [Q14CB8-3]
DR ProteomicsDB; 60320; -. [Q14CB8-4]
DR ProteomicsDB; 60321; -. [Q14CB8-5]
DR ProteomicsDB; 60322; -. [Q14CB8-6]
DR ProteomicsDB; 60323; -. [Q14CB8-7]
DR Antibodypedia; 30829; 140 antibodies from 20 providers.
DR DNASU; 84986; -.
DR Ensembl; ENST00000358308.7; ENSP00000351058.4; ENSG00000213390.11. [Q14CB8-6]
DR Ensembl; ENST00000358531.9; ENSP00000351333.4; ENSG00000213390.11. [Q14CB8-1]
DR Ensembl; ENST00000371027.5; ENSP00000360066.1; ENSG00000213390.11. [Q14CB8-3]
DR GeneID; 84986; -.
DR KEGG; hsa:84986; -.
DR MANE-Select; ENST00000358531.9; ENSP00000351333.4; NM_032900.6; NP_116289.4.
DR UCSC; uc001kna.5; human. [Q14CB8-1]
DR CTD; 84986; -.
DR DisGeNET; 84986; -.
DR GeneCards; ARHGAP19; -.
DR HGNC; HGNC:23724; ARHGAP19.
DR HPA; ENSG00000213390; Tissue enhanced (lymphoid).
DR MIM; 611587; gene.
DR neXtProt; NX_Q14CB8; -.
DR OpenTargets; ENSG00000213390; -.
DR OpenTargets; ENSG00000269891; -.
DR PharmGKB; PA134917415; -.
DR VEuPathDB; HostDB:ENSG00000213390; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00940000157331; -.
DR HOGENOM; CLU_046228_0_0_1; -.
DR InParanoid; Q14CB8; -.
DR OMA; CQSPANQ; -.
DR OrthoDB; 878646at2759; -.
DR PhylomeDB; Q14CB8; -.
DR TreeFam; TF326309; -.
DR PathwayCommons; Q14CB8; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q14CB8; -.
DR SIGNOR; Q14CB8; -.
DR BioGRID-ORCS; 84986; 24 hits in 1069 CRISPR screens.
DR GeneWiki; ARHGAP19; -.
DR GenomeRNAi; 84986; -.
DR Pharos; Q14CB8; Tbio.
DR PRO; PR:Q14CB8; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q14CB8; protein.
DR Bgee; ENSG00000213390; Expressed in trigeminal ganglion and 169 other tissues.
DR ExpressionAtlas; Q14CB8; baseline and differential.
DR Genevisible; Q14CB8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; GTPase activation; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..494
FT /note="Rho GTPase-activating protein 19"
FT /id="PRO_0000280465"
FT DOMAIN 102..308
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 349..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BRH3"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..382
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_023695"
FT VAR_SEQ 1..19
FT /note="MATEAQSEGEVPARESGRS -> MPHQKLSALI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023696"
FT VAR_SEQ 281..309
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023697"
FT VAR_SEQ 281..301
FT /note="VTANDLQENITKLNSGMAFMI -> GLVLLPTLEESNTITTHCSLI (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_023698"
FT VAR_SEQ 302..494
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_023699"
FT VAR_SEQ 332..346
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_023700"
FT VAR_SEQ 493..494
FT /note="FL -> NSMATTSLGSIRMTLRGSSSCGCCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17454002"
FT /id="VSP_023701"
FT VARIANT 305
FT /note="Q -> R (in dbSNP:rs17112598)"
FT /id="VAR_031152"
FT CONFLICT 28
FT /note="C -> Y (in Ref. 1; AAR02412/ABC69298)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="E -> A (in Ref. 4; CAH18254)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="E -> G (in Ref. 2; BAC04165)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="S -> L (in Ref. 2; BAC04165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 55756 MW; EAE8DF3FD1253858 CRC64;
MATEAQSEGE VPARESGRSD AICSFVICND SSLRGQPIIF NPDFFVEKLR HEKPEIFTEL
VVSNITRLID LPGTELAQLM GEVDLKLPGG AGPASGFFRS LMSLKRKEKG VIFGSPLTEE
GIAQIYQLIE YLHKNLRVEG LFRVPGNSVR QQILRDALNN GTDIDLESGE FHSNDVATLL
KMFLGELPEP LLTHKHFNAH LKIADLMQFD DKGNKTNIPD KDRQIEALQL LFLILPPPNR
NLLKLLLDLL YQTAKKQDKN KMSAYNLALM FAPHVLWPKN VTANDLQENI TKLNSGMAFM
IKHSQKLFKA PAYIRECARL HYLGSRTQAS KDDLDLIASC HTKSFQLAKS QKRNRVDSCP
HQEETQHHTE EALRELFQHV HDMPESAKKK QLIRQFNKQS LTQTPGREPS TSQVQKRARS
RSFSGLIKRK VLGNQMMSEK KKKNPTPESV AIGELKGTSK ENRNLLFSGS PAVTMTPTRL
KWSEGKKEGK KGFL
