RGPS2_HUMAN
ID RGPS2_HUMAN Reviewed; 583 AA.
AC Q86X27; B7Z7B1; Q5T5Z1; Q5VZ67; Q9NW78;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ras-specific guanine nucleotide-releasing factor RalGPS2;
DE AltName: Full=Ral GEF with PH domain and SH3-binding motif 2;
DE AltName: Full=RalA exchange factor RalGPS2;
GN Name=RALGPS2;
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] (ISOFORMS 2 AND 3).
RC TISSUE=Embryo, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [5]
RP POSSIBLE INVOLVEMENT IN ALZHEIMER DISEASE.
RX PubMed=17564960; DOI=10.1086/518720;
RA Liu F., Arias-Vasquez A., Sleegers K., Aulchenko Y.S., Kayser M.,
RA Sanchez-Juan P., Feng B.J., Bertoli-Avella A.M., van Swieten J.,
RA Axenovich T.I., Heutink P., van Broeckhoven C., Oostra B.A.,
RA van Duijn C.M.;
RT "A genomewide screen for late-onset Alzheimer disease in a genetically
RT isolated Dutch population.";
RL Am. J. Hum. Genet. 81:17-31(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-311; THR-326 AND
RP SER-329, AND 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326 AND SER-329, AND
RP IDENTIFICATION BY 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-329; SER-343;
RP THR-361; SER-374 AND SER-422, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326; SER-329 AND THR-361, AND
RP IDENTIFICATION BY 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: Guanine nucleotide exchange factor for the small GTPase RALA.
CC May be involved in cytoskeletal organization. May also be involved in
CC the stimulation of transcription in a Ras-independent fashion (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the SH3 domains of GRB2 and PLCG1. Interacts
CC with RALA. {ECO:0000250}.
CC -!- INTERACTION:
CC Q86X27; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-1050841, EBI-1051317;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Associates with membranes through the PH domain.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86X27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86X27-2; Sequence=VSP_031971;
CC Name=3;
CC IsoId=Q86X27-3; Sequence=VSP_054909;
CC -!- DOMAIN: The PH domain mediates binding to phosphatidylinositol 4,5-
CC bisphosphate. {ECO:0000250}.
CC -!- DISEASE: Note=RALGPS2 is a potential candidate gene for susceptibility
CC to Alzheimer disease linked to 1q24. {ECO:0000269|PubMed:17564960}.
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DR EMBL; AK001106; BAA91506.1; -; mRNA.
DR EMBL; AK301753; BAH13547.1; -; mRNA.
DR EMBL; AL162255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91028.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91029.1; -; Genomic_DNA.
DR EMBL; BC047391; AAH47391.1; -; mRNA.
DR CCDS; CCDS1325.1; -. [Q86X27-1]
DR CCDS; CCDS65733.1; -. [Q86X27-3]
DR RefSeq; NP_001273176.1; NM_001286247.1. [Q86X27-3]
DR RefSeq; NP_689876.2; NM_152663.4. [Q86X27-1]
DR RefSeq; XP_006711473.1; XM_006711410.3. [Q86X27-1]
DR AlphaFoldDB; Q86X27; -.
DR SMR; Q86X27; -.
DR BioGRID; 120413; 48.
DR IntAct; Q86X27; 11.
DR MINT; Q86X27; -.
DR STRING; 9606.ENSP00000356607; -.
DR GlyGen; Q86X27; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86X27; -.
DR PhosphoSitePlus; Q86X27; -.
DR BioMuta; RALGPS2; -.
DR DMDM; 74750518; -.
DR EPD; Q86X27; -.
DR jPOST; Q86X27; -.
DR MassIVE; Q86X27; -.
DR MaxQB; Q86X27; -.
DR PaxDb; Q86X27; -.
DR PeptideAtlas; Q86X27; -.
DR PRIDE; Q86X27; -.
DR ProteomicsDB; 70228; -. [Q86X27-1]
DR ProteomicsDB; 70229; -. [Q86X27-2]
DR Antibodypedia; 34414; 101 antibodies from 17 providers.
DR DNASU; 55103; -.
DR Ensembl; ENST00000367634.7; ENSP00000356606.2; ENSG00000116191.19. [Q86X27-3]
DR Ensembl; ENST00000367635.8; ENSP00000356607.3; ENSG00000116191.19. [Q86X27-1]
DR GeneID; 55103; -.
DR KEGG; hsa:55103; -.
DR MANE-Select; ENST00000367635.8; ENSP00000356607.3; NM_152663.5; NP_689876.2.
DR UCSC; uc001glz.5; human. [Q86X27-1]
DR CTD; 55103; -.
DR DisGeNET; 55103; -.
DR GeneCards; RALGPS2; -.
DR HGNC; HGNC:30279; RALGPS2.
DR HPA; ENSG00000116191; Tissue enhanced (lymphoid tissue, testis).
DR MIM; 617819; gene.
DR neXtProt; NX_Q86X27; -.
DR NIAGADS; ENSG00000116191; -.
DR OpenTargets; ENSG00000116191; -.
DR PharmGKB; PA134864387; -.
DR VEuPathDB; HostDB:ENSG00000116191; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000154079; -.
DR HOGENOM; CLU_021333_0_1_1; -.
DR InParanoid; Q86X27; -.
DR OMA; HVSFWTV; -.
DR OrthoDB; 343666at2759; -.
DR PhylomeDB; Q86X27; -.
DR TreeFam; TF352150; -.
DR PathwayCommons; Q86X27; -.
DR SignaLink; Q86X27; -.
DR BioGRID-ORCS; 55103; 10 hits in 1089 CRISPR screens.
DR ChiTaRS; RALGPS2; human.
DR GenomeRNAi; 55103; -.
DR Pharos; Q86X27; Tdark.
DR PRO; PR:Q86X27; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86X27; protein.
DR Bgee; ENSG00000116191; Expressed in gingival epithelium and 168 other tissues.
DR ExpressionAtlas; Q86X27; baseline and differential.
DR Genevisible; Q86X27; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0032485; P:regulation of Ral protein signal transduction; IEA:InterPro.
DR CDD; cd00155; RasGEF; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR030708; RalGPS1/2.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR PANTHER; PTHR23113:SF180; PTHR23113:SF180; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Alzheimer disease; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..583
FT /note="Ras-specific guanine nucleotide-releasing factor
FT RalGPS2"
FT /id="PRO_0000322600"
FT DOMAIN 49..287
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 457..569
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 283..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..583
FT /note="Required for stimulation of nucleotide exchange by
FT RALA"
FT /evidence="ECO:0000250"
FT MOTIF 324..327
FT /note="PXXP"
FT COMPBIAS 383..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERD6"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERD6"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 280..583
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031971"
FT VAR_SEQ 416..441
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054909"
FT VARIANT 225
FT /note="N -> S (in dbSNP:rs35161510)"
FT /id="VAR_039468"
FT CONFLICT 395
FT /note="I -> V (in Ref. 1; BAH13547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 65167 MW; B6D85A8ACBEBED15 CRC64;
MDLMNGQASS VNIAATASEK SSSSESLSDK GSELKKSFDA VVFDVLKVTP EEYAGQITLM
DVPVFKAIQP DELSSCGWNK KEKYSSAPNA VAFTRRFNHV SFWVVREILH AQTLKIRAEV
LSHYIKTAKK LYELNNLHAL MAVVSGLQSA PIFRLTKTWA LLSRKDKTTF EKLEYVMSKE
DNYKRLRDYI SSLKMTPCIP YLGIYLSDLT YIDSAYPSTG SILENEQRSN LMNNILRIIS
DLQQSCEYDI PMLPHVQKYL NSVQYIEELQ KFVEDDNYKL SLKIEPGTST PRSAASREDL
VGPEVGASPQ SGRKSVAAEG ALLPQTPPSP RNLIPHGHRK CHSLGYNFIH KMNTAEFKSA
TFPNAGPRHL LDDSVMEPHA PSRGQAESST LSSGISIGSS DGSELSEETS WPAFERNRLY
HSLGPVTRVA RNGYRSHMKA SSSAESEDLA VHLYPGAVTI QGVLRRKTLL KEGKKPTVAS
WTKYWAALCG TQLFYYAAKS LKATERKHFK STSNKNVSVI GWMVMMADDP EHPDLFLLTD
SEKGNSYKFQ AGNRMNAMLW FKHLSAACQS NKQQVPTNLM TFE
