RASL1_HUMAN
ID RASL1_HUMAN Reviewed; 804 AA.
AC O95294; B7ZKM4; C9JFK5; F8VQX1; Q52M03; Q59H24; Q96CC7;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=RasGAP-activating-like protein 1 {ECO:0000305};
DE AltName: Full=RAS protein activator like 1 {ECO:0000312|HGNC:HGNC:9873};
DE AltName: Full=Ras GTPase-activating-like protein {ECO:0000303|PubMed:9751798};
GN Name=RASAL1 {ECO:0000312|HGNC:HGNC:9873};
GN Synonyms=RASAL {ECO:0000303|PubMed:9751798};
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 HIS-321, PROBABLE FUNCTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=9751798; DOI=10.1016/s0378-1119(98)00394-1;
RA Allen M., Chu S., Brill S., Stotler C., Buckler A.;
RT "Restricted tissue expression pattern of a novel human rasGAP-related gene
RT and its murine ortholog.";
RL Gene 218:17-25(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT HIS-321.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/2/4), AND VARIANTS
RP LEU-11; MET-58 AND HIS-321.
RC TISSUE=Brain, and Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-700 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA Yoon T.J.;
RT "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT differentiation.";
RL J. Dermatol. Sci. 72:246-251(2013).
CC -!- FUNCTION: Probable inhibitory regulator of the Ras-cyclic AMP pathway
CC (PubMed:9751798). Plays a role in dendrite formation by melanocytes
CC (PubMed:23999003). {ECO:0000269|PubMed:23999003,
CC ECO:0000269|PubMed:9751798}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95294-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95294-2; Sequence=VSP_001627;
CC Name=3;
CC IsoId=O95294-3; Sequence=VSP_047005, VSP_047006;
CC Name=4;
CC IsoId=O95294-4; Sequence=VSP_047006;
CC -!- TISSUE SPECIFICITY: Highly expressed in thyroid and adrenal medulla,
CC lower expression in brain, spinal cord and trachea (PubMed:9751798).
CC Expressed in melanocytes (PubMed:23999003).
CC {ECO:0000269|PubMed:23999003, ECO:0000269|PubMed:9751798}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92172.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF086713; AAD09006.1; -; mRNA.
DR EMBL; AB208935; BAD92172.1; ALT_INIT; mRNA.
DR EMBL; AC089999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014420; AAH14420.1; -; mRNA.
DR EMBL; BC093724; AAH93724.1; -; mRNA.
DR EMBL; BC143261; AAI43262.1; -; mRNA.
DR EMBL; AL136672; CAB66607.2; -; Transcribed_RNA.
DR CCDS; CCDS55888.1; -. [O95294-2]
DR CCDS; CCDS55889.1; -. [O95294-3]
DR CCDS; CCDS73529.1; -. [O95294-4]
DR CCDS; CCDS9165.1; -. [O95294-1]
DR RefSeq; NP_001180449.1; NM_001193520.1. [O95294-3]
DR RefSeq; NP_001180450.1; NM_001193521.1. [O95294-2]
DR RefSeq; NP_001288131.1; NM_001301202.1. [O95294-4]
DR RefSeq; NP_004649.2; NM_004658.2. [O95294-1]
DR RefSeq; XP_005254007.1; XM_005253950.4. [O95294-3]
DR RefSeq; XP_006719704.1; XM_006719641.3. [O95294-3]
DR RefSeq; XP_011537154.1; XM_011538852.2. [O95294-3]
DR RefSeq; XP_011537155.1; XM_011538853.2. [O95294-1]
DR RefSeq; XP_016875517.1; XM_017020028.1. [O95294-4]
DR AlphaFoldDB; O95294; -.
DR SMR; O95294; -.
DR BioGRID; 114017; 5.
DR STRING; 9606.ENSP00000450244; -.
DR iPTMnet; O95294; -.
DR PhosphoSitePlus; O95294; -.
DR SwissPalm; O95294; -.
DR BioMuta; RASAL1; -.
DR EPD; O95294; -.
DR jPOST; O95294; -.
DR MassIVE; O95294; -.
DR MaxQB; O95294; -.
DR PaxDb; O95294; -.
DR PeptideAtlas; O95294; -.
DR PRIDE; O95294; -.
DR ProteomicsDB; 28360; -.
DR ProteomicsDB; 50790; -. [O95294-1]
DR ProteomicsDB; 50791; -. [O95294-2]
DR Antibodypedia; 31222; 239 antibodies from 32 providers.
DR DNASU; 8437; -.
DR Ensembl; ENST00000261729.9; ENSP00000261729.5; ENSG00000111344.12. [O95294-1]
DR Ensembl; ENST00000446861.7; ENSP00000395920.3; ENSG00000111344.12. [O95294-2]
DR Ensembl; ENST00000546530.5; ENSP00000450244.1; ENSG00000111344.12. [O95294-3]
DR Ensembl; ENST00000548055.2; ENSP00000448510.1; ENSG00000111344.12. [O95294-4]
DR GeneID; 8437; -.
DR KEGG; hsa:8437; -.
DR MANE-Select; ENST00000548055.2; ENSP00000448510.1; NM_001301202.2; NP_001288131.1. [O95294-4]
DR UCSC; uc001tul.4; human. [O95294-1]
DR CTD; 8437; -.
DR DisGeNET; 8437; -.
DR GeneCards; RASAL1; -.
DR HGNC; HGNC:9873; RASAL1.
DR HPA; ENSG00000111344; Tissue enhanced (parathyroid gland, salivary gland).
DR MIM; 604118; gene.
DR neXtProt; NX_O95294; -.
DR OpenTargets; ENSG00000111344; -.
DR PharmGKB; PA34234; -.
DR VEuPathDB; HostDB:ENSG00000111344; -.
DR eggNOG; KOG2059; Eukaryota.
DR GeneTree; ENSGT00940000158715; -.
DR HOGENOM; CLU_008096_0_0_1; -.
DR InParanoid; O95294; -.
DR OMA; HQQDVKY; -.
DR OrthoDB; 145372at2759; -.
DR PhylomeDB; O95294; -.
DR TreeFam; TF105302; -.
DR PathwayCommons; O95294; -.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR BioGRID-ORCS; 8437; 9 hits in 1058 CRISPR screens.
DR ChiTaRS; RASAL1; human.
DR GenomeRNAi; 8437; -.
DR Pharos; O95294; Tbio.
DR PRO; PR:O95294; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O95294; protein.
DR Bgee; ENSG00000111344; Expressed in lower esophagus mucosa and 139 other tissues.
DR Genevisible; O95294; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd05135; RasGAP_RASAL; 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; IPR028555; RASAL1.
DR InterPro; IPR037776; RASAL_RasGAP.
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 PANTHER; PTHR10194:SF3; PTHR10194:SF3; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
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; Differentiation; GTPase activation;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..804
FT /note="RasGAP-activating-like protein 1"
FT /id="PRO_0000056645"
FT DOMAIN 1..105
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 116..231
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 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 149
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 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 458
FT /note="Q -> QQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047005"
FT VAR_SEQ 552
FT /note="E -> EE (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.2"
FT /id="VSP_047006"
FT VAR_SEQ 610..637
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001627"
FT VARIANT 11
FT /note="V -> L (in dbSNP:rs7960087)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031665"
FT VARIANT 58
FT /note="T -> M (in dbSNP:rs34598602)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031666"
FT VARIANT 321
FT /note="R -> H (in dbSNP:rs1284879)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9751798, ECO:0000269|Ref.2"
FT /id="VAR_031667"
FT CONFLICT 141
FT /note="Q -> H (in Ref. 1; AAD09006)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="L -> P (in Ref. 5; CAB66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="Q -> R (in Ref. 5; CAB66607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 804 AA; 90016 MW; 5D0065A093487FD0 CRC64;
MAKSSSLNVR VVEGRALPAK DVSGSSDPYC LVKVDDEVVA RTATVWRSLG PFWGEEYTVH
LPLDFHQLAF YVLDEDTVGH DDIIGKISLS REAITADPRG IDSWINLSRV DPDAEVQGEI
CLSVQMLEDG QGRCLRCHVL QARDLAPRDI SGTSDPFARV FWGSQSLETS TIKKTRFPHW
DEVLELREMP GAPSPLRVEL WDWDMVGKND FLGMVEFSPK TLQQKPPKGW FRLLPFPRAE
EDSGGNLGAL RVKVRLIEDR VLPSQCYQPL MELLMESVQG PAEEDTASPL ALLEELTLGD
CRQDLATKLV KLFLGRGLAG RFLDYLTRRE VARTMDPNTL FRSNSLASKS MEQFMKLVGM
PYLHEVLKPV ISRVFEEKKY MELDPCKMDL GRTRRISFKG ALSEEQMRET SLGLLTGYLG
PIVDAIVGSV GRCPPAMRLA FKQLHRRVEE RFPQAEHQDV KYLAISGFLF LRFFAPAILT
PKLFDLRDQH ADPQTSRSLL LLAKAVQSIG NLGQQLGQGK ELWMAPLHPF LLQCVSRVRD
FLDRLVDVDG DEAGVPARAL FPPSAIVREG YLLKRKEEPA GLATRFAFKK RYVWLSGETL
SFSKSPEWQM CHSIPVSHIR AVERVDEGAF QLPHVMQVVT QDGTGALHTT YLQCKNVNEL
NQWLSALRKA SAPNPNKLAA CHPGAFRSAR WTCCLQAERS AAGCSRTHSA VTLGDWSDPL
DPDAEAQTVY RQLLLGRDQL RLKLLEDSNM DTTLEADTGA CPEVLARQRA ATARLLEVLA
DLDRAHEEFQ QQERGKAALG PLGP
