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   24-JAN-2024, entry version 158.
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; 29.
DR   IntAct; Q86YV0; 24.
DR   STRING; 9606.ENSP00000341905; -.
DR   GlyGen; Q86YV0; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000341905; -.
DR   PeptideAtlas; Q86YV0; -.
DR   ProteomicsDB; 70473; -. [Q86YV0-1]
DR   ProteomicsDB; 70474; -. [Q86YV0-2]
DR   Antibodypedia; 54246; 86 antibodies from 16 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   AGR; HGNC:26129; -.
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; TWGSRSQ; -.
DR   OrthoDB; 22721at2759; -.
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; 12 hits in 1150 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 158 other cell types or tissues.
DR   ExpressionAtlas; Q86YV0; baseline and differential.
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   CDD; cd13374; PH_RASAL3; 1.
DR   CDD; cd05136; RasGAP_DAB2IP; 1.
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; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   PANTHER; PTHR10194:SF96; RAS PROTEIN ACTIVATOR LIKE-3; 1.
DR   Pfam; PF00616; RasGAP; 2.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   Genevisible; Q86YV0; HS.
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
//