RASL2_HUMAN
ID RASL2_HUMAN Reviewed; 803 AA.
AC O43374; O60286; Q14CQ4; Q86UW3; Q96QU0;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 185.
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, GAPL, KIAA0538;
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 [MRNA] (ISOFORM 1), VARIANT VAL-352, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Blood;
RX PubMed=11448776; DOI=10.1016/s0960-9822(01)00261-5;
RA Lockyer P.J., Kupzig S., Cullen P.J.;
RT "CAPRI regulates Ca(2+)-dependent inactivation of the Ras-MAPK pathway.";
RL Curr. Biol. 11:981-986(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-352.
RC TISSUE=Liver;
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).
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. {ECO:0000269|PubMed:11448776}.
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 {ECO:0000269|PubMed:11448776}.
CC Cell membrane {ECO:0000269|PubMed:11448776}; Peripheral membrane
CC protein {ECO:0000269|PubMed:11448776}. Note=Localized to the cytosol as
CC a result of its lack of phosphoinositide binding activity. Upon
CC agonist-stimulated calcium mobilization, utilizes the C2A and C2B
CC domains to associate with the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43374-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43374-2; Sequence=VSP_039965;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11448776}.
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-592, compared to Arg found in other
CC family members.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB97935.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAP22345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA25464.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY029206; AAK31582.1; -; mRNA.
DR EMBL; AB011110; BAA25464.2; ALT_INIT; mRNA.
DR EMBL; AK026441; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC004084; AAB97935.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC093668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105052; AAP22345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC113663; AAI13664.1; -; mRNA.
DR CCDS; CCDS47674.1; -. [O43374-2]
DR CCDS; CCDS5725.1; -. [O43374-1]
DR RefSeq; NP_001073346.2; NM_001079877.2. [O43374-2]
DR RefSeq; NP_008920.5; NM_006989.5. [O43374-1]
DR AlphaFoldDB; O43374; -.
DR SMR; O43374; -.
DR BioGRID; 115458; 4.
DR IntAct; O43374; 7.
DR MINT; O43374; -.
DR STRING; 9606.ENSP00000262940; -.
DR iPTMnet; O43374; -.
DR PhosphoSitePlus; O43374; -.
DR BioMuta; RASA4; -.
DR EPD; O43374; -.
DR jPOST; O43374; -.
DR MassIVE; O43374; -.
DR MaxQB; O43374; -.
DR PaxDb; O43374; -.
DR PeptideAtlas; O43374; -.
DR PRIDE; O43374; -.
DR ProteomicsDB; 48913; -. [O43374-1]
DR ProteomicsDB; 48914; -. [O43374-2]
DR Antibodypedia; 31113; 103 antibodies from 22 providers.
DR DNASU; 10156; -.
DR Ensembl; ENST00000262940.12; ENSP00000262940.8; ENSG00000105808.19. [O43374-1]
DR Ensembl; ENST00000449970.6; ENSP00000412876.2; ENSG00000105808.19. [O43374-2]
DR GeneID; 10156; -.
DR KEGG; hsa:10156; -.
DR MANE-Select; ENST00000262940.12; ENSP00000262940.8; NM_006989.6; NP_008920.5.
DR UCSC; uc003vae.4; human. [O43374-1]
DR CTD; 10156; -.
DR DisGeNET; 10156; -.
DR GeneCards; RASA4; -.
DR HGNC; HGNC:23181; RASA4.
DR HPA; ENSG00000105808; Group enriched (skeletal muscle, tongue).
DR MIM; 607943; gene.
DR neXtProt; NX_O43374; -.
DR OpenTargets; ENSG00000105808; -.
DR PharmGKB; PA134889495; -.
DR VEuPathDB; HostDB:ENSG00000105808; -.
DR eggNOG; KOG2059; Eukaryota.
DR GeneTree; ENSGT00940000160149; -.
DR HOGENOM; CLU_008096_0_0_1; -.
DR InParanoid; O43374; -.
DR OMA; CKCMNEL; -.
DR OrthoDB; 145372at2759; -.
DR PhylomeDB; O43374; -.
DR TreeFam; TF105302; -.
DR PathwayCommons; O43374; -.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR SignaLink; O43374; -.
DR BioGRID-ORCS; 10156; 212 hits in 984 CRISPR screens.
DR ChiTaRS; RASA4; human.
DR GeneWiki; RASA4; -.
DR GenomeRNAi; 10156; -.
DR Pharos; O43374; Tbio.
DR PRO; PR:O43374; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O43374; protein.
DR Bgee; ENSG00000105808; Expressed in hindlimb stylopod muscle and 97 other tissues.
DR ExpressionAtlas; O43374; baseline and differential.
DR Genevisible; O43374; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:CACAO.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; 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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; GTPase activation;
KW Membrane; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..803
FT /note="Ras GTPase-activating protein 4"
FT /id="PRO_0000056647"
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 302..512
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 566..673
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 675..711
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT REGION 781..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 683
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 695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT VAR_SEQ 611..656
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039965"
FT VARIANT 352
FT /note="M -> V (in dbSNP:rs144395384)"
FT /evidence="ECO:0000269|PubMed:11448776,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027680"
FT VARIANT 432
FT /note="R -> P (in dbSNP:rs886346)"
FT /id="VAR_027681"
FT CONFLICT 213
FT /note="G -> V (in Ref. 3; AK026441)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> G (in Ref. 3; AK026441)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="R -> L (in Ref. 3; AK026441)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="M -> V (in Ref. 3; AK026441)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="T -> M (in Ref. 2; BAA25464)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="A -> T (in Ref. 2; BAA25464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 803 AA; 90458 MW; 6E70DBF2F8F5D0E9 CRC64;
MAKRSSLYIR IVEGKNLPAK DITGSSDPYC IVKVDNEPII RTATVWKTLC PFWGEEYQVH
LPPTFHAVAF YVMDEDALSR DDVIGKVCLT RDTIASHPKG FSGWAHLTEV DPDEEVQGEI
HLRLEVWPGA RACRLRCSVL EARDLAPKDR NGTSDPFVRV RYKGRTRETS IVKKSCYPRW
NETFEFELQE GAMEALCVEA WDWDLVSRND FLGKVVIDVQ RLRVVQQEEG WFRLQPDQSK
SRRHDEGNLG SLQLEVRLRD ETVLPSSYYQ PLVHLLCHEV KLGMQGPGQL IPLIEETTST
ECRQDVATNL LKLFLGQGLA KDFLDLLFQL ELSRTSETNT LFRSNSLASK SMESFLKVAG
MQYLHGVLGP IINKVFEEKK YVELDPSKVE VKDVGCSGLH RPQTEAEVLE QSAQTLRAHL
GALLSALSRS VRACPAVVRA TFRQLFRRVR ERFPGAQHEN VPFIAVTSFL CLRFFSPAIM
SPKLFHLRER HADARTSRTL LLLAKAVQNV GNMDTPASRA KEAWMEPLQP TVRQGVAQLK
DFITKLVDIE EKDELDLQRT LSLQAPPVKE GPLFIHRTKG KGPLMSSSFK KLYFSLTTEA
LSFAKTPSSK KSALIKLANI RAAEKVEEKS FGGSHVMQVI YTDDAGRPQT AYLQCKCVNE
LNQWLSALRK VSINNTGLLG SYHPGVFRGD KWSCCHQKEK TGQGCDKTRS RVTLQEWNDP
LDHDLEAQLI YRHLLGVEAM LWERHRELSG GAEAGTVPTS PGKVPEDSLA RLLRVLQDLR
EAHSSSPAGS PPSEPNCLLE LQT
