RASL3_HUMAN
ID RASL3_HUMAN Reviewed; 1011 AA.
AC Q86YV0; Q8N2T9; Q9H735;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=RAS protein activator like-3;
GN Name=RASAL3;
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=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-1011 (ISOFORM 2).
RC TISSUE=Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-1011 (ISOFORM 1).
RC TISSUE=Blood;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-164; SER-167 AND
RP SER-231, AND 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-988, 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).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25652366; DOI=10.1002/eji.201444977;
RA Saito S., Kawamura T., Higuchi M., Kobayashi T., Yoshita-Takahashi M.,
RA Yamazaki M., Abe M., Sakimura K., Kanda Y., Kawamura H., Jiang S.,
RA Naito M., Yoshizaki T., Takahashi M., Fujii M.;
RT "RASAL3, a novel hematopoietic RasGAP protein, regulates the number and
RT functions of NKT cells.";
RL Eur. J. Immunol. 45:1512-1523(2015).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Functions as a Ras GTPase-activating protein. Plays an
CC important role in the expansion and functions of natural killer T (NKT)
CC cells in the liver by negatively regulating RAS activity and the down-
CC stream ERK signaling pathway. {ECO:0000250|UniProtKB:Q8C2K5}.
CC -!- INTERACTION:
CC Q86YV0; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-3437896, EBI-746752;
CC Q86YV0; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-3437896, EBI-742722;
CC Q86YV0; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-3437896, EBI-10171570;
CC Q86YV0; Q86X02: CDR2L; NbExp=3; IntAct=EBI-3437896, EBI-11063830;
CC Q86YV0; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-3437896, EBI-745369;
CC Q86YV0; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-3437896, EBI-7060731;
CC Q86YV0; Q86YM7: HOMER1; NbExp=3; IntAct=EBI-3437896, EBI-746815;
CC Q86YV0; O75525: KHDRBS3; NbExp=3; IntAct=EBI-3437896, EBI-722504;
CC Q86YV0; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-3437896, EBI-3044087;
CC Q86YV0; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-3437896, EBI-11522433;
CC Q86YV0; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-3437896, EBI-741158;
CC Q86YV0; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3437896, EBI-79165;
CC Q86YV0; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-3437896, EBI-1105153;
CC Q86YV0; P54646: PRKAA2; NbExp=3; IntAct=EBI-3437896, EBI-1383852;
CC Q86YV0; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-3437896, EBI-14093916;
CC Q86YV0; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-3437896, EBI-3437896;
CC Q86YV0; Q9Y272: RASD1; NbExp=3; IntAct=EBI-3437896, EBI-740818;
CC Q86YV0; P09012: SNRPA; NbExp=3; IntAct=EBI-3437896, EBI-607085;
CC Q86YV0; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-3437896, EBI-11952721;
CC Q86YV0; Q9UPY6-2: WASF3; NbExp=3; IntAct=EBI-3437896, EBI-12026286;
CC Q86YV0; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-3437896, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25652366}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:25652366}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86YV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YV0-2; Sequence=VSP_033824;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in cells of hematopoietic
CC lineages. {ECO:0000269|PubMed:25652366}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15064.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC56928.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC56928.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122587; BAC56928.1; ALT_SEQ; mRNA.
DR EMBL; AC011492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK025091; BAB15064.1; ALT_INIT; mRNA.
DR EMBL; BC030281; AAH30281.1; ALT_INIT; mRNA.
DR CCDS; CCDS46006.1; -. [Q86YV0-1]
DR RefSeq; NP_001334956.1; NM_001348027.1.
DR RefSeq; NP_001334957.1; NM_001348028.1.
DR RefSeq; NP_075055.1; NM_022904.2. [Q86YV0-1]
DR AlphaFoldDB; Q86YV0; -.
DR SMR; Q86YV0; -.
DR BioGRID; 122348; 26.
DR IntAct; Q86YV0; 25.
DR STRING; 9606.ENSP00000341905; -.
DR iPTMnet; Q86YV0; -.
DR MetOSite; Q86YV0; -.
DR PhosphoSitePlus; Q86YV0; -.
DR BioMuta; RASAL3; -.
DR DMDM; 172046741; -.
DR EPD; Q86YV0; -.
DR jPOST; Q86YV0; -.
DR MassIVE; Q86YV0; -.
DR MaxQB; Q86YV0; -.
DR PaxDb; Q86YV0; -.
DR PeptideAtlas; Q86YV0; -.
DR PRIDE; Q86YV0; -.
DR ProteomicsDB; 70473; -. [Q86YV0-1]
DR ProteomicsDB; 70474; -. [Q86YV0-2]
DR Antibodypedia; 54246; 71 antibodies from 15 providers.
DR DNASU; 64926; -.
DR Ensembl; ENST00000343625.12; ENSP00000341905.5; ENSG00000105122.13. [Q86YV0-1]
DR GeneID; 64926; -.
DR KEGG; hsa:64926; -.
DR MANE-Select; ENST00000343625.12; ENSP00000341905.5; NM_022904.3; NP_075055.1.
DR UCSC; uc002nbe.3; human. [Q86YV0-1]
DR CTD; 64926; -.
DR DisGeNET; 64926; -.
DR GeneCards; RASAL3; -.
DR HGNC; HGNC:26129; RASAL3.
DR HPA; ENSG00000105122; Group enriched (bone marrow, intestine, lung, lymphoid tissue).
DR MIM; 616561; gene.
DR neXtProt; NX_Q86YV0; -.
DR OpenTargets; ENSG00000105122; -.
DR PharmGKB; PA164725297; -.
DR VEuPathDB; HostDB:ENSG00000105122; -.
DR eggNOG; KOG3508; Eukaryota.
DR GeneTree; ENSGT00940000161423; -.
DR HOGENOM; CLU_009167_0_0_1; -.
DR InParanoid; Q86YV0; -.
DR OMA; WGRHKSP; -.
DR OrthoDB; 69536at2759; -.
DR PhylomeDB; Q86YV0; -.
DR TreeFam; TF105303; -.
DR PathwayCommons; Q86YV0; -.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR SignaLink; Q86YV0; -.
DR BioGRID-ORCS; 64926; 11 hits in 1071 CRISPR screens.
DR ChiTaRS; RASAL3; human.
DR GenomeRNAi; 64926; -.
DR Pharos; Q86YV0; Tbio.
DR PRO; PR:Q86YV0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86YV0; protein.
DR Bgee; ENSG00000105122; Expressed in granulocyte and 157 other tissues.
DR ExpressionAtlas; Q86YV0; baseline and differential.
DR Genevisible; Q86YV0; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:UniProtKB.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194; PTHR10194; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1011
FT /note="RAS protein activator like-3"
FT /id="PRO_0000322566"
FT DOMAIN 197..293
FT /note="PH"
FT DOMAIN 284..404
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 458..650
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 888..988
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 944..1011
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033824"
FT VARIANT 251
FT /note="L -> V (in dbSNP:rs58123634)"
FT /id="VAR_061179"
FT VARIANT 594
FT /note="R -> C (in dbSNP:rs56209154)"
FT /id="VAR_061180"
FT VARIANT 825
FT /note="P -> T (in dbSNP:rs57208996)"
FT /id="VAR_061181"
SQ SEQUENCE 1011 AA; 111898 MW; 23A7CA251ED3CE33 CRC64;
MDPPSPSRTS QTQPTATSPL TSYRWHTGGG GEKAAGGFRW GRFAGWGRAL SHQEPMVSTQ
PAPRSIFRRV LSAPPKESRT SRLRLSKALW GRHKNPPPEP DPEPEQEAPE LEPEPELEPP
TPQIPEAPTP NVPVWDIGGF TLLDGKLVLL GGEEEGPRRP RVGSASSEGS IHVAMGNFRD
PDRMPGKTEP ETAGPNQVHN VRGLLKRLKE KKKARLEPRD GPPSALGSRE SLATLSELDL
GAERDVRIWP LHPSLLGEPH CFQVTWTGGS RCFSCRSAAE RDRWIEDLRR QFQPTQDNVE
REETWLSVWV HEAKGLPRAA AGAPGVRAEL WLDGALLART APRAGPGQLF WAERFHFEAL
PPARRLSLRL RGLGPGSAVL GRVALALEEL DAPRAPAAGL ERWFPLLGAP AGAALRARIR
ARRLRVLPSE RYKELAEFLT FHYARLCGAL EPALPAQAKE ELAAAMVRVL RATGRAQALV
TDLGTAELAR CGGREALLFR ENTLATKAID EYMKLVAQDY LQETLGQVVR RLCASTEDCE
VDPSKCPASE LPEHQARLRN SCEEVFETII HSYDWFPAEL GIVFSSWREA CKERGSEVLG
PRLVCASLFL RLLCPAILAP SLFGLAPDHP APGPARTLTL IAKVIQNLAN RAPFGEKEAY
MGFMNSFLEE HGPAMQCFLD QVAMVDVDAA PSGYQGSGDL ALQLAVLHAQ LCTIFAELDQ
TTRDTLEPLP TILRAIEEGQ PVLVSVPMRL PLPPAQVHSS LSAGEKPGFL APRDLPKHTP
LISKSQSLRS VRRSESWARP RPDEERPLRR PRPVQRTQSV PVRRPARRRQ SAGPWPRPKG
SLSMGPAPRA RPWTRDSASL PRKPSVPWQR QMDQPQDRNQ ALGTHRPVNK LAELQCEVAA
LREEQKVLSR LVESLSTQIR ALTEQQEQLR GQLQDLDSRL RAGSSEFDSE HNLTSNEGHS
LKNLEHRLNE MERTQAQLRD AVQSLQLSPR TRGSWSQPQP LKAPCLNGDT T
