RGPA1_MOUSE
ID RGPA1_MOUSE Reviewed; 2035 AA.
AC Q6GYP7; Q6GYP6; Q6ZQ28; Q8BNJ5; Q8C9G8; Q8CIW4; Q9JMC4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ral GTPase-activating protein subunit alpha-1;
DE AltName: Full=GAP-related-interacting partner to E12;
DE Short=GRIPE;
DE AltName: Full=GTPase-activating RapGAP domain-like 1;
DE AltName: Full=Tuberin-like protein 1;
DE AltName: Full=p240;
GN Name=Ralgapa1; Synonyms=Garnl1, Kiaa0884, Tulip1;
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 1S), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH TCF3/E12.
RC STRAIN=C57BL/6J; TISSUE=Forebrain;
RX PubMed=12200424; DOI=10.1074/jbc.m204858200;
RA Heng J.I.T., Tan S.-S.;
RT "Cloning and characterization of GRIPE, a novel interacting partner of the
RT transcription factor E12 in developing mouse forebrain.";
RL J. Biol. Chem. 277:43152-43159(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ;
RX PubMed=15498464; DOI=10.1016/j.ygeno.2004.04.013;
RA Schwarzbraun T., Vincent J.B., Schumacher A., Geschwind D.H., Oliveira J.,
RA Windpassinger C., Ofner L., Ledinegg M.K., Kroisel P.M., Wagner K.,
RA Petek E.;
RT "Cloning, genomic structure and expression profile of TULIP1 (GARNL1), a
RT brain-expressed candidate gene for 14q13-linked neurological phenotypes and
RT its murine homolog.";
RL Genomics 84:577-586(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 PROTEIN SEQUENCE OF 339-350, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-860, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-753; SER-772; SER-859;
RP SER-860; SER-863 AND THR-1001, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
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: Catalytic subunit of the heterodimeric RalGAP1 complex which
CC acts as a GTPase activator for the Ras-like small GTPases RALA and RALB
CC (By similarity). May interact with the HLH region of TCF3/isoform E12.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the heterodimeric RalGAP1 complex with RALGAPB.
CC Heterodimerization is required for activity (By similarity). Interacts
CC with the HLH region of TCF3/isoform E12. {ECO:0000250,
CC ECO:0000269|PubMed:12200424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12200424}. Nucleus
CC {ECO:0000269|PubMed:12200424}. Note=Translocated to the nucleus, when
CC associated with TCF3/E12.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=3;
CC IsoId=Q6GYP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6GYP7-2; Sequence=VSP_011338;
CC Name=4;
CC IsoId=Q6GYP7-3; Sequence=VSP_011332, VSP_011335;
CC Name=5;
CC IsoId=Q6GYP7-4; Sequence=VSP_011333, VSP_011334;
CC Name=6;
CC IsoId=Q6GYP7-5; Sequence=VSP_011331, VSP_011336, VSP_011337;
CC Name=1S;
CC IsoId=Q6GYP7-6; Sequence=VSP_011330;
CC -!- TISSUE SPECIFICITY: Expressed during embryogenesis. Expressed in the
CC adult brain, particularly in neurons of the cortex and hippocampus.
CC {ECO:0000269|PubMed:12200424}.
CC -!- DEVELOPMENTAL STAGE: Expression decreased during development, but
CC persists in the adult brain.
CC -!- MISCELLANEOUS: [Isoform 1S]: May be a partial isoform 1. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to act as a transcriptional regulator
CC via its interaction with TCF3/E12. {ECO:0000305|PubMed:12200424}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92774.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98046.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY066011; AAL47577.1; -; mRNA.
DR EMBL; AY596972; AAT49273.1; -; mRNA.
DR EMBL; AY596973; AAT49274.1; -; mRNA.
DR EMBL; AY596974; AAT49275.1; -; mRNA.
DR EMBL; AK129236; BAC98046.1; ALT_INIT; mRNA.
DR EMBL; AB032400; BAA92774.1; ALT_SEQ; mRNA.
DR EMBL; AK042116; BAC31171.1; -; mRNA.
DR EMBL; AK083518; BAC38939.1; -; mRNA.
DR CCDS; CCDS36452.1; -. [Q6GYP7-1]
DR RefSeq; NP_001003719.1; NM_001003719.2.
DR RefSeq; NP_001106185.1; NM_001112714.2. [Q6GYP7-1]
DR RefSeq; NP_001273192.1; NM_001286263.1.
DR RefSeq; NP_064378.4; NM_019994.5. [Q6GYP7-1]
DR AlphaFoldDB; Q6GYP7; -.
DR SMR; Q6GYP7; -.
DR BioGRID; 208171; 14.
DR IntAct; Q6GYP7; 1.
DR STRING; 10090.ENSMUSP00000106315; -.
DR iPTMnet; Q6GYP7; -.
DR PhosphoSitePlus; Q6GYP7; -.
DR EPD; Q6GYP7; -.
DR jPOST; Q6GYP7; -.
DR MaxQB; Q6GYP7; -.
DR PaxDb; Q6GYP7; -.
DR PeptideAtlas; Q6GYP7; -.
DR PRIDE; Q6GYP7; -.
DR ProteomicsDB; 254933; -. [Q6GYP7-1]
DR ProteomicsDB; 254934; -. [Q6GYP7-2]
DR ProteomicsDB; 254935; -. [Q6GYP7-3]
DR ProteomicsDB; 254936; -. [Q6GYP7-4]
DR ProteomicsDB; 254937; -. [Q6GYP7-5]
DR ProteomicsDB; 254938; -. [Q6GYP7-6]
DR Antibodypedia; 79; 85 antibodies from 20 providers.
DR DNASU; 56784; -.
DR Ensembl; ENSMUST00000085385; ENSMUSP00000082503; ENSMUSG00000021027. [Q6GYP7-1]
DR Ensembl; ENSMUST00000110687; ENSMUSP00000106315; ENSMUSG00000021027. [Q6GYP7-1]
DR GeneID; 56784; -.
DR KEGG; mmu:56784; -.
DR UCSC; uc007nou.2; mouse. [Q6GYP7-1]
DR UCSC; uc007nov.2; mouse. [Q6GYP7-2]
DR UCSC; uc007now.1; mouse. [Q6GYP7-5]
DR UCSC; uc007nox.2; mouse. [Q6GYP7-4]
DR CTD; 253959; -.
DR MGI; MGI:1931050; Ralgapa1.
DR VEuPathDB; HostDB:ENSMUSG00000021027; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00950000183139; -.
DR HOGENOM; CLU_001676_0_0_1; -.
DR InParanoid; Q6GYP7; -.
DR OrthoDB; 157372at2759; -.
DR PhylomeDB; Q6GYP7; -.
DR TreeFam; TF324484; -.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR BioGRID-ORCS; 56784; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ralgapa1; mouse.
DR PRO; PR:Q6GYP7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6GYP7; protein.
DR Bgee; ENSMUSG00000021027; Expressed in ascending aorta and 232 other tissues.
DR ExpressionAtlas; Q6GYP7; baseline and differential.
DR Genevisible; Q6GYP7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR027107; Tuberin/Ral-act_asu.
DR PANTHER; PTHR10063; PTHR10063; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Direct protein sequencing;
KW GTPase activation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..2035
FT /note="Ral GTPase-activating protein subunit alpha-1"
FT /id="PRO_0000056754"
FT DOMAIN 1795..2003
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 343..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..2035
FT /note="Minimal domain that binds to TCF3/E12"
FT COILED 1713..1748
FT /evidence="ECO:0000255"
FT COMPBIAS 348..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 753
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 777
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55007"
FT MOD_RES 1001
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55007"
FT MOD_RES 1477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55007"
FT VAR_SEQ 1..1337
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011331"
FT VAR_SEQ 1..1298
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011332"
FT VAR_SEQ 1..555
FT /note="Missing (in isoform 1S)"
FT /evidence="ECO:0000303|PubMed:12200424"
FT /id="VSP_011330"
FT VAR_SEQ 1035..1037
FT /note="EIS -> GNA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011333"
FT VAR_SEQ 1038..2035
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011334"
FT VAR_SEQ 1299..1304
FT /note="WICEEL -> MMRFVE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011335"
FT VAR_SEQ 1897..1904
FT /note="LRHLGNDE -> VSAEGKHF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011336"
FT VAR_SEQ 1905..2035
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011337"
FT VAR_SEQ 2034..2035
FT /note="DH -> VGSYPEIPPSDAAPAAQVDGADLASPMSPRTSKSR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498464"
FT /id="VSP_011338"
FT CONFLICT 420
FT /note="L -> V (in Ref. 3; BAC98046)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="L -> S (in Ref. 1; AAL47577)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="P -> L (in Ref. 1; AAL47577)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="E -> V (in Ref. 1; AAL47577)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="D -> G (in Ref. 1; AAL47577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1166
FT /note="D -> N (in Ref. 1; AAL47577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1365
FT /note="I -> V (in Ref. 4; BAA92774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1398
FT /note="I -> T (in Ref. 4; BAA92774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1494
FT /note="T -> P (in Ref. 4; BAA92774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1586
FT /note="G -> S (in Ref. 4; BAA92774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1634
FT /note="Q -> P (in Ref. 4; BAA92774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1638
FT /note="E -> K (in Ref. 4; BAA92774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1674
FT /note="R -> Q (in Ref. 4; BAA92774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1775..1780
FT /note="SWDKRR -> WAAGIPGTNGG (in Ref. 1; AAL47577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1966..1968
FT /note="VLP -> SSA (in Ref. 1; AAL47577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2035 AA; 229389 MW; 1F4C3E24022EBB54 CRC64;
MFSKKPHGDV KKSTQKVLDT KKDALTRLKH LRIVIENAES IDLKQFFDQH FSHIYYVFFE
NFVTIEASLK QKGHKSQREE LDAILFIFEK ILQLLPERIH QRWQFHSIGL ILKKLLHTGN
SLKIRREGVR LFLLWLQALQ DNCSKEQLWM FSCLIPGFSA PQSEYGPRTL DNLINPPLSL
QETQVTIEEV TPLVPPQSGD KGQEDLTSYF LEALLKYIVI QVKSLEWKNK ENQERGFSFL
FSHFKKFYLP YIFPNICKEN SLYHPVLDIP QIRPKPHYVM IKKDAETNET IYCTKEPFIQ
ARVIVIRWLV SFWLEPKPHS GPNIPGMEGE VLPKNIQRAA ASLVSREESK NDTVDKVDKS
AEPEQSHSNT STLTEREPSS SSLCSIDEEH LTDIEIVRRV FSSKRSNVNF VTEIFRQAFL
LPICEAAAMR KVVKVYQEWI QQEEKPLFMQ EPEDTAITCS DIPCSETVAD HDSAIEDGEK
REEENGTSTS EHVRNSSWTK NGSYQEAFHV CEEATEQNIQ AGTQAVLQVF IINSSNIFLL
EPANEIKNLL DEHTDMCKRI LNIYRYMVVQ VSMDKKTWEQ MLLVLLRVTE SVLKMSSQAF
LQFQGKKSMT LAGRLAGPLF QTLIVAWIKA NLNVYISREL WDDLLSVLSS LTYWEELATE
WSLTMETLTK VLARNLYSLD LSDLPLDKLS EQKQKKHKGK GVGHEFQKVS VDKSFSRGWS
RDQPGQAPMR QRSATTTGSP GTEKARSIVR QKTVDIDDAQ ILPRSTRVRH FSQSEDTGNE
VFGALHEEQP LPRSSSTSDI LEPFTVERAK VNKEDTSPKL PPLNSETGGN SANVPDLMDE
FIAERLRSGN ASTMTRRGSS PGSLEIPKDL PDILNKQNQM RPVDDPGVPS EWTSPASAGS
SDLMSSDSHS DSFSAFQCEG RKFDNFGFGT DIGIPSSADV DLGSGHHQST EEQEVASLTT
LHLDSETSSL NQQAFSAEVA TVTGSESASP VHSALGSRSQ TPSPSTLSRA HIEQKDLQLD
EKLHHSVLQT PDDLEISEFP SECCSVMAGG TLTGWHADVA TVMWRRMLGI LGDVNAIMDP
EIHAQVFDYL CELWQNLAKI RDNLGISADN LTSPSPPVLI PPLRILTPWL FKATMLTDKY
KQGKLHAYKL ICNTMKRRQD VSPNRDFLTH FYNIMHCGLL HIDQDIVNTI IKHCSPQFFS
LGLPGATMLI MDFIIAAGRV ASSAFLNAPR VEAQVLLGSL VCFPNLYCEL PALHPNIPDI
AVSQFTDVKE LIIKTVLSSA RDEPSGPARC VALCSLGIWI CEELVHESHH PQIKEALNVI
CVSLKFTNKT VAHVACNMLH MLVHYVPRLQ IHQPQSPLKI IQILIATITH LLPSTEASSY
EMDKRLVVSL LLCLLDWIMA LPLKTLLQPV HATGAENDKT EKSVLNCIYK VLHGCVYGAQ
SFSNPKYFPI SLSDLASVDY DPFMHLESLK EPEPLHSPDS ERSSKLQPVT EVKTQMQQGL
ISIAARTVIT HLVNHLGHYP MSGGPAMLTS QVCENHDNHY SESTELSPEL FESPNIQFFV
LNNTTLVSCI QIRSEESMPG GGLAAGLVSA NSNVRIIVRD LSGKYSWDSA ILYGPPIVSG
LPEPTSFILS MSDQEKPEEP PTSNECLEDI AVKDGLSLQL RRFRETVPTW STIREEEDVL
DELLQYLGTT SPECLQRTGI SLNVPAPQPL CISEKQENDV INAILKQYTE EKEFVEKHFN
DLNMKASEQD EPTPQKPQSA FYYCRLLLSI LGMNSWDKRR SFHLLKKNEK LLRELRNLDS
RQCRETHKIA VFYVAEGQED KYSILTNIGG SQAYEDFVAG LGWEVNLTNH CGFMGGLQKN
RSTGLTTPYF ATSTVEVIFH VSTRMPSDSD DSLTKKLRHL GNDEVHIVWS EHTRDYRRGI
IPTEFGDVLI VIYPMKNHMF SIQIMKKPEV PFFGPLFDGA IVNGKVLPIM VRSTAINASR
ALKSLIPLYQ NFYEERARYL QTIVQHHLEP TTFEDFAAQV FSPAPYHHFP ADADH
