RASL2_MOUSE
ID RASL2_MOUSE Reviewed; 802 AA.
AC Q6PFQ7; Q2PMI6; Q3U2R4; Q571H1; Q58DY7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ras GTPase-activating protein 4;
DE AltName: Full=Calcium-promoted Ras inactivator;
DE AltName: Full=Ras p21 protein activator 4;
DE AltName: Full=RasGAP-activating-like protein 2;
GN Name=Rasa4; Synonyms=Capri, Kiaa0538;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16041389; DOI=10.1038/ni1232;
RA Zhang J., Guo J., Dzhagalov I., He Y.W.;
RT "An essential function for the calcium-promoted Ras inactivator in Fcgamma
RT receptor-mediated phagocytosis.";
RL Nat. Immunol. 6:911-919(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BC8;
RX PubMed=16234249; DOI=10.1074/jbc.m507000200;
RA Hikita A., Kadono Y., Chikuda H., Fukuda A., Wakeyama H., Yasuda H.,
RA Nakamura K., Oda H., Miyazaki T., Tanaka S.;
RT "Identification of an alternatively spliced variant of Ca2+-promoted Ras
RT inactivator as a possible regulator of RANKL shedding.";
RL J. Biol. Chem. 280:41700-41706(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches
CC off the Ras-MAPK pathway following a stimulus that elevates
CC intracellular calcium. Functions as an adaptor for Cdc42 and Rac1
CC during FcR-mediated phagocytosis. Isoform 2 activates the Ras pathway
CC and promotes RANKL shedding by modulating the expression of MMP14.
CC {ECO:0000269|PubMed:16041389, ECO:0000269|PubMed:16234249}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral
CC membrane protein. Note=Localized to the cytosol as a result of its lack
CC of phosphoinositide binding activity. Upon agonist-stimulated calcium
CC mobilization, utilizes the C2A and C2B domains to associate with the
CC plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PFQ7-1; Sequence=Displayed;
CC Name=2; Synonyms=deltaCAPRI;
CC IsoId=Q6PFQ7-2; Sequence=VSP_032042;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in osteoblasts.
CC {ECO:0000269|PubMed:16234249}.
CC -!- DOMAIN: The PH domain does not bind phosphatidylinositol 4,5-
CC bisphosphate or phosphatidylinositol 3,4,5-trisphosphate. This lack of
CC binding activity is due to Leu-591, compared to Arg found in other
CC family members (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY591339; AAT00515.1; -; mRNA.
DR EMBL; DQ317932; ABC47038.1; -; mRNA.
DR EMBL; AK220218; BAD90143.1; ALT_INIT; mRNA.
DR EMBL; AK154335; BAE32521.1; -; mRNA.
DR EMBL; AK155146; BAE33076.1; -; mRNA.
DR EMBL; BC057460; AAH57460.1; -; mRNA.
DR EMBL; BC092143; AAH92143.1; -; mRNA.
DR CCDS; CCDS39324.1; -. [Q6PFQ7-1]
DR CCDS; CCDS39325.1; -. [Q6PFQ7-2]
DR RefSeq; NP_001034192.1; NM_001039103.3. [Q6PFQ7-2]
DR RefSeq; NP_598675.2; NM_133914.3. [Q6PFQ7-1]
DR AlphaFoldDB; Q6PFQ7; -.
DR SMR; Q6PFQ7; -.
DR STRING; 10090.ENSMUSP00000037869; -.
DR iPTMnet; Q6PFQ7; -.
DR PhosphoSitePlus; Q6PFQ7; -.
DR EPD; Q6PFQ7; -.
DR MaxQB; Q6PFQ7; -.
DR PaxDb; Q6PFQ7; -.
DR PeptideAtlas; Q6PFQ7; -.
DR PRIDE; Q6PFQ7; -.
DR ProteomicsDB; 254989; -. [Q6PFQ7-1]
DR ProteomicsDB; 254990; -. [Q6PFQ7-2]
DR DNASU; 54153; -.
DR Ensembl; ENSMUST00000042135; ENSMUSP00000037869; ENSMUSG00000004952. [Q6PFQ7-1]
DR Ensembl; ENSMUST00000100570; ENSMUSP00000098136; ENSMUSG00000004952. [Q6PFQ7-2]
DR GeneID; 54153; -.
DR KEGG; mmu:54153; -.
DR UCSC; uc008zzt.2; mouse. [Q6PFQ7-1]
DR UCSC; uc008zzu.2; mouse. [Q6PFQ7-2]
DR CTD; 10156; -.
DR MGI; MGI:1858600; Rasa4.
DR VEuPathDB; HostDB:ENSMUSG00000004952; -.
DR eggNOG; KOG2059; Eukaryota.
DR GeneTree; ENSGT00940000160149; -.
DR HOGENOM; CLU_008096_0_0_1; -.
DR InParanoid; Q6PFQ7; -.
DR OMA; CKCMNEL; -.
DR OrthoDB; 145372at2759; -.
DR PhylomeDB; Q6PFQ7; -.
DR TreeFam; TF105302; -.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR BioGRID-ORCS; 54153; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Rasa4; mouse.
DR PRO; PR:Q6PFQ7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6PFQ7; protein.
DR Bgee; ENSMUSG00000004952; Expressed in primary oocyte and 115 other tissues.
DR ExpressionAtlas; Q6PFQ7; baseline and differential.
DR Genevisible; Q6PFQ7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd13372; PH_CAPRI; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR037777; RASA4_PH.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR PANTHER; PTHR10194; PTHR10194; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; GTPase activation;
KW Membrane; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..802
FT /note="Ras GTPase-activating protein 4"
FT /id="PRO_0000323606"
FT DOMAIN 1..105
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 116..232
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 301..511
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 565..672
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 674..710
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 704
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT VAR_SEQ 459..504
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16234249"
FT /id="VSP_032042"
FT CONFLICT 208
FT /note="R -> Q (in Ref. 3; BAD90143)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="A -> V (in Ref. 3; BAD90143)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="S -> I (in Ref. 4; BAE33076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 802 AA; 90060 MW; 185EBA11B2384099 CRC64;
MAKRSSLSIR IVEGKNLPAK DITGSSDPYC IVKVDNEPII RTATVWKTLC PFWGEDYQVH
LPPTFHTVAF YVMDEDALSR DDVIGKVCLT RDALASHPKG FSGWTHLVEV DPNEEVQGEI
HLRLEVVPGV HASRLRCAVL EARDLAPKDR NGASDPFVRV HYNGRTQETS VVKKSCYPRW
NETFDFELEK GASEALLVEA WDWDLVSRND FLGKVAVNVQ RLCSAQQEEG WFRLQPDQSK
SRQGKGNLGS LQLEVRLRDE TVLPSVCYQP LVQLLCQEVK LGTQGPGRLI PVIEETTSAE
CRQEVATTLL KLFLGQGLAK DFLDLLFQLE LGRTSEANTL FRSNSLASKS MESFLKVAGM
RYLHGILGPI IDRVFEEKKY VELDPSKVEV KDVGCSGLHR PQTEAEVLEQ SAQTLRAHLV
ALLSAICRSV RTCPAIIRAT FRQLFRRVRE RFPNAQHQNV PFIAVTSFLC LRFFSPAILS
PKLFHLRERH ADARTSRTLL LLAKAVQNIG NMDTPVSRAK ESWMEPLQPT VRQGVAQLKD
FIMKLVDIEE KEELDLQRAL NSQAPPVKEG PLFIHRTKGK GPLASSSFKK LYFSLTTEAL
SFAKTSSSKK STFIKLASIR AAEKVEEKSF GSSHIMQVIY ADDVGRAQTV YLQCKCVNEL
NQWLSALRKA STNNRGLLRS YHPGIFRGDK WSCCHQKDKT DQGCDKTHSR VTLQEWNDPL
DHDLEAQLIY RHLLGVEAAL RERYQLLRGA TEAGVSPTGC DGAPEDSLAQ LLRVLQDLRE
AHGSSLASPA AREPHHLLEL QT
