RLGPB_HUMAN
ID RLGPB_HUMAN Reviewed; 1494 AA.
AC Q86X10; A2A2E8; A2A2E9; Q5TG31; Q8N3D1; Q8WWC0; Q9H3X8; Q9UJR1; Q9ULK1;
AC Q9Y3G9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ral GTPase-activating protein subunit beta;
DE AltName: Full=p170;
GN Name=RALGAPB; Synonyms=KIAA1219;
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 3).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Melanoma;
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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-1494 (ISOFORM 4).
RC TISSUE=Tongue;
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 [8]
RP INTERACTION WITH RALGAPA2.
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-734, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; THR-379 AND SER-720, 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Non-catalytic subunit of the heterodimeric RalGAP1 and
CC RalGAP2 complexes which act as GTPase activators for the Ras-like small
CC GTPases RALA and RALB. {ECO:0000250}.
CC -!- SUBUNIT: Component of the heterodimeric RalGAP1 complex with RALGAPA1
CC and of the heterodimeric RalGAP2 complex with RALGAPA2.
CC Heterodimerization is required for activity (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q86X10; Q9HD26-2: GOPC; NbExp=3; IntAct=EBI-1755842, EBI-11102276;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86X10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86X10-2; Sequence=VSP_009693, VSP_009696;
CC Name=3;
CC IsoId=Q86X10-3; Sequence=VSP_009694, VSP_009696;
CC Name=4;
CC IsoId=Q86X10-4; Sequence=VSP_009695;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, mostly in amygdala.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Splicing acceptor site is not canonical.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86533.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85649.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB61346.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD39096.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033045; BAA86533.3; ALT_INIT; mRNA.
DR EMBL; AL834436; CAD39096.1; ALT_INIT; mRNA.
DR EMBL; AL132998; CAB61346.1; ALT_INIT; mRNA.
DR EMBL; AL035419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010916; AAH10916.2; -; mRNA.
DR EMBL; BC018668; AAH18668.1; -; mRNA.
DR EMBL; BC047482; AAH47482.1; -; mRNA.
DR EMBL; AK123576; BAC85649.1; ALT_INIT; mRNA.
DR CCDS; CCDS13305.1; -. [Q86X10-1]
DR CCDS; CCDS63272.1; -. [Q86X10-3]
DR RefSeq; NP_001269846.1; NM_001282917.1. [Q86X10-1]
DR RefSeq; NP_001269847.1; NM_001282918.1. [Q86X10-3]
DR RefSeq; NP_065069.1; NM_020336.3. [Q86X10-1]
DR AlphaFoldDB; Q86X10; -.
DR BioGRID; 121405; 59.
DR IntAct; Q86X10; 26.
DR MINT; Q86X10; -.
DR STRING; 9606.ENSP00000262879; -.
DR GlyGen; Q86X10; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86X10; -.
DR PhosphoSitePlus; Q86X10; -.
DR BioMuta; RALGAPB; -.
DR DMDM; 45477126; -.
DR EPD; Q86X10; -.
DR jPOST; Q86X10; -.
DR MassIVE; Q86X10; -.
DR MaxQB; Q86X10; -.
DR PaxDb; Q86X10; -.
DR PeptideAtlas; Q86X10; -.
DR PRIDE; Q86X10; -.
DR ProteomicsDB; 195; -.
DR ProteomicsDB; 70218; -. [Q86X10-1]
DR ProteomicsDB; 70219; -. [Q86X10-2]
DR ProteomicsDB; 70220; -. [Q86X10-3]
DR ProteomicsDB; 70221; -. [Q86X10-4]
DR Antibodypedia; 62413; 27 antibodies from 11 providers.
DR DNASU; 57148; -.
DR Ensembl; ENST00000262879.11; ENSP00000262879.6; ENSG00000170471.15. [Q86X10-1]
DR Ensembl; ENST00000397040.5; ENSP00000380233.1; ENSG00000170471.15. [Q86X10-1]
DR Ensembl; ENST00000397042.7; ENSP00000380235.3; ENSG00000170471.15. [Q86X10-3]
DR GeneID; 57148; -.
DR KEGG; hsa:57148; -.
DR MANE-Select; ENST00000262879.11; ENSP00000262879.6; NM_020336.4; NP_065069.1.
DR UCSC; uc002xiw.5; human. [Q86X10-1]
DR CTD; 57148; -.
DR DisGeNET; 57148; -.
DR GeneCards; RALGAPB; -.
DR HGNC; HGNC:29221; RALGAPB.
DR HPA; ENSG00000170471; Low tissue specificity.
DR MIM; 618833; gene.
DR neXtProt; NX_Q86X10; -.
DR OpenTargets; ENSG00000170471; -.
DR PharmGKB; PA165392608; -.
DR VEuPathDB; HostDB:ENSG00000170471; -.
DR eggNOG; KOG3652; Eukaryota.
DR GeneTree; ENSGT00700000104550; -.
DR HOGENOM; CLU_005005_1_0_1; -.
DR InParanoid; Q86X10; -.
DR OMA; ANMAEEQ; -.
DR OrthoDB; 54832at2759; -.
DR PhylomeDB; Q86X10; -.
DR TreeFam; TF324460; -.
DR PathwayCommons; Q86X10; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR SignaLink; Q86X10; -.
DR BioGRID-ORCS; 57148; 54 hits in 1088 CRISPR screens.
DR ChiTaRS; RALGAPB; human.
DR GeneWiki; KIAA1219; -.
DR GenomeRNAi; 57148; -.
DR Pharos; Q86X10; Tbio.
DR PRO; PR:Q86X10; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q86X10; protein.
DR Bgee; ENSG00000170471; Expressed in buccal mucosa cell and 202 other tissues.
DR ExpressionAtlas; Q86X10; baseline and differential.
DR Genevisible; Q86X10; HS.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR039930; RALGAPB.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR PANTHER; PTHR21344; PTHR21344; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1494
FT /note="Ral GTPase-activating protein subunit beta"
FT /id="PRO_0000056756"
FT DOMAIN 1149..1392
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 355..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..737
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 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P86410"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQZ4"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_009693"
FT VAR_SEQ 749..752
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10574462"
FT /id="VSP_009694"
FT VAR_SEQ 943..1473
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009695"
FT VAR_SEQ 1233
FT /note="E -> EE (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_009696"
FT CONFLICT 326
FT /note="P -> S (in Ref. 1; CAD39096)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072
FT /note="Y -> G (in Ref. 6; AAH18668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1494 AA; 166799 MW; 5FEDBB0CB269F8CE CRC64;
MYSEWRSLHL VIQNDQGHTS VLHSYPESVG REVANAVVRP LGQVLGTPSV AGSENLLKTD
KEVKWTMEVI CYGLTLPLDG ETVKYCVDVY TDWIMALVLP KDSIPLPVIK EPNQYVQTIL
KHLQNLFVPR QEQGSSQIRL CLQVLRAIQK LARESSLMAR ETWEVLLLFL LQINDILLAP
PTVQGGIAEN LAEKLIGVLF EVWLLACTRC FPTPPYWKTA KEMVANWRHH PAVVEQWSKV
ICALTSRLLR FTYGPSFPAF KVPDEDASLI PPEMDNECVA QTWFRFLHML SNPVDLSNPA
IISSTPKFQE QFLNVSGMPQ ELNQYPCLKH LPQIFFRAMR GISCLVDAFL GISRPRSDSA
PPTPVNRLSM PQSAAVSTTP PHNRRHRAVT VNKATMKTST VSTAHASKVQ HQTSSTSPLS
SPNQTSSEPR PLPAPRRPKV NSILNLFGSW LFDAAFVHCK LHNGINRDSS MTAITTQASM
EFRRKGSQMS TDTMVSNPMF DASEFPDNYE AGRAEACGTL CRIFCSKKTG EEILPAYLSR
FYMLLIQGLQ INDYVCHPVL ASVILNSPPL FCCDLKGIDV VVPYFISALE TILPDRELSK
FKSYVNPTEL RRSSINILLS LLPLPHHFGT VKSEVVLEGK FSNDDSSSYD KPITFLSLKL
RLVNILIGAL QTETDPNNTQ MILGAMLNIV QDSALLEAIG CQMEMGGGEN NLKSHSRTNS
GISSASGGST EPTTPDSERP AQALLRDYAL NTDSAAGLLI RSIHLVTQRL NSQWRQDMSI
SLAALELLSG LAKVKVMVDS GDRKRAISSV CTYIVYQCSR PAPLHSRDLH SMIVAAFQCL
CVWLTEHPDM LDEKDCLKEV LEIVELGISG SKSKNNEQEV KYKGDKEPNP ASMRVKDAAE
ATLTCIMQLL GAFPSPSGPA SPCSLVNETT LIKYSRLPTI NKHSFRYFVL DNSVILAMLE
QPLGNEQNDF FPSVTVLVRG MSGRLAWAQQ LCLLPRGAKA NQKLFVPEPR PVPKNDVGFK
YSVKHRPFPE EVDKIPFVKA DLSIPDLHEI VTEELEERHE KLRSGMAQQI AYEIHLEQQS
EEELQKRSFP DPVTDCKPPP PAQEFQTARL FLSHFGFLSL EALKEPANSR LPPHLIALDS
TIPGFFDDIG YLDLLPCRPF DTVFIFYMKP GQKTNQEILK NVESSRTVQP HFLEFLLSLG
WSVDVGRHPG WTGHVSTSWS INCCDDGEGS QQEVISSEDI GASIFNGQKK VLYYADALTE
IAFVVPSPVE SLTDSLESNI SDQDSDSNMD LMPGILKQPS LTLELFPNHT DNLNSSQRLS
PSSRMRKLPQ GRPVPPLGPE TRVSVVWVER YDDIENFPLS ELMTEISTGV ETTANSSTSL
RSTTLEKEVP VIFIHPLNTG LFRIKIQGAT GKFNMVIPLV DGMIVSRRAL GFLVRQTVIN
ICRRKRLESD SYSPPHVRRK QKITDIVNKY RNKQLEPEFY TSLFQEVGLK NCSS
