RIN1_HUMAN
ID RIN1_HUMAN Reviewed; 783 AA.
AC Q13671; O15010; Q00427; Q96CC8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ras and Rab interactor 1;
DE AltName: Full=Ras inhibitor JC99;
DE AltName: Full=Ras interaction/interference protein 1;
GN Name=RIN1;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Glial cell;
RX PubMed=1849280; DOI=10.1073/pnas.88.7.2913;
RA Colicelli J., Nicolette C., Birchmeier C., Rodgers L., Riggs M., Wigler M.;
RT "Expression of three mammalian cDNAs that interfere with RAS function in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2913-2917(1991).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7862125; DOI=10.1128/mcb.15.3.1318;
RA Han L., Colicelli J.;
RT "A human protein selected for interference with Ras function interacts
RT directly with Ras and competes with Raf1.";
RL Mol. Cell. Biol. 15:1318-1323(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RIN1 AND RIN1-DELTA), SEQUENCE
RP REVISION, FUNCTION, DOMAINS, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Glioblastoma;
RX PubMed=9144171; DOI=10.1073/pnas.94.10.4954;
RA Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., Herschman H.,
RA Witte O., Colicelli J.;
RT "Protein binding and signaling properties of RIN1 suggest a unique effector
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 FUNCTION, INTERACTION WITH ABL1, AND PHOSPHORYLATION BY ABL1.
RX PubMed=9208849; DOI=10.1016/s1074-7613(00)80452-5;
RA Afar D.E.H., Han L., McLaughlin J., Wong S., Dhaka A., Parmar K.,
RA Rosenberg N., Witte O.N., Colicelli J.;
RT "Regulation of the oncogenic activity of BCR-ABL by a tightly bound
RT substrate protein RIN1.";
RL Immunity 6:773-782(1997).
RN [6]
RP GEF ACTIVITY.
RX PubMed=11703925; DOI=10.1016/s1534-5807(01)00008-9;
RA Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F.;
RT "Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide
RT exchange activity of RIN1.";
RL Dev. Cell 1:73-82(2001).
RN [7]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-351, AND MUTAGENESIS OF
RP SER-351.
RX PubMed=11784866; DOI=10.1128/mcb.22.3.916-926.2001;
RA Wang Y., Waldron R.T., Dhaka A., Patel A., Riley M.M., Rozengurt E.,
RA Colicelli J.;
RT "The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-
RT 3 proteins.";
RL Mol. Cell. Biol. 22:916-926(2002).
RN [8]
RP FUNCTION, INTERACTION WITH ABL1 AND ABL2, AND PHOSPHORYLATION AT TYR-36.
RX PubMed=15886098; DOI=10.1016/j.cub.2005.03.049;
RA Hu H., Bliss J.M., Wang Y., Colicelli J.;
RT "RIN1 is an ABL tyrosine kinase activator and a regulator of epithelial-
RT cell adhesion and migration.";
RL Curr. Biol. 15:815-823(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-337, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-258; SER-337;
RP SER-351 AND SER-609, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3; SER-16 AND SER-337, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-351; SER-609 AND
RP SER-611, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-692, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Ras effector protein, which may serve as an inhibitory
CC modulator of neuronal plasticity in aversive memory formation. Can
CC affect Ras signaling at different levels. First, by competing with RAF1
CC protein for binding to activated Ras. Second, by enhancing signaling
CC from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by
CC activating RAB5A, possibly by functioning as a guanine nucleotide
CC exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP,
CC and facilitating Ras-activated receptor endocytosis.
CC {ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:9144171,
CC ECO:0000269|PubMed:9208849}.
CC -!- SUBUNIT: Interacts with the GTP-bound form of Ras proteins (NRAS, HRAS
CC and KRAS). This interaction prevents the association between RAF1 and
CC Ras. Interacts with 14-3-3 proteins YWHAB, YWHAE and YWHAZ when
CC phosphorylated on Ser-351. Interacts with the SH3 domain of ABL1 and
CC ABL2. Interacts with RAB5A. The interaction with Ras is probably
CC regulated and antagonized by the interaction with 14-3-3 proteins. The
CC interaction with 14-3-3 proteins is regulated by phosphorylation on
CC Ser-351. {ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:9208849}.
CC -!- INTERACTION:
CC Q13671; P00519: ABL1; NbExp=4; IntAct=EBI-366017, EBI-375543;
CC Q13671; P42684: ABL2; NbExp=5; IntAct=EBI-366017, EBI-1102694;
CC Q13671; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-366017, EBI-11954519;
CC Q13671; Q7Z6G8-3: ANKS1B; NbExp=3; IntAct=EBI-366017, EBI-17714371;
CC Q13671; Q13137: CALCOCO2; NbExp=4; IntAct=EBI-366017, EBI-739580;
CC Q13671; Q96L46: CAPNS2; NbExp=3; IntAct=EBI-366017, EBI-12188723;
CC Q13671; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-366017, EBI-3866279;
CC Q13671; Q9BSQ5: CCM2; NbExp=3; IntAct=EBI-366017, EBI-1573056;
CC Q13671; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-366017, EBI-11982645;
CC Q13671; P00533: EGFR; NbExp=3; IntAct=EBI-366017, EBI-297353;
CC Q13671; O00303: EIF3F; NbExp=3; IntAct=EBI-366017, EBI-711990;
CC Q13671; P21860: ERBB3; NbExp=2; IntAct=EBI-366017, EBI-720706;
CC Q13671; Q08379: GOLGA2; NbExp=3; IntAct=EBI-366017, EBI-618309;
CC Q13671; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-366017, EBI-5916454;
CC Q13671; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-366017, EBI-740641;
CC Q13671; P01112: HRAS; NbExp=6; IntAct=EBI-366017, EBI-350145;
CC Q13671; O75031: HSF2BP; NbExp=3; IntAct=EBI-366017, EBI-7116203;
CC Q13671; Q53G59: KLHL12; NbExp=3; IntAct=EBI-366017, EBI-740929;
CC Q13671; O76011: KRT34; NbExp=3; IntAct=EBI-366017, EBI-1047093;
CC Q13671; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-366017, EBI-11992140;
CC Q13671; Q9BRK4: LZTS2; NbExp=9; IntAct=EBI-366017, EBI-741037;
CC Q13671; Q99750: MDFI; NbExp=3; IntAct=EBI-366017, EBI-724076;
CC Q13671; P01111: NRAS; NbExp=9; IntAct=EBI-366017, EBI-721993;
CC Q13671; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-366017, EBI-79165;
CC Q13671; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-366017, EBI-949255;
CC Q13671; P62070: RRAS2; NbExp=4; IntAct=EBI-366017, EBI-491037;
CC Q13671; Q15437: SEC23B; NbExp=3; IntAct=EBI-366017, EBI-742673;
CC Q13671; Q15036: SNX17; NbExp=3; IntAct=EBI-366017, EBI-1752620;
CC Q13671; O60504: SORBS3; NbExp=3; IntAct=EBI-366017, EBI-741237;
CC Q13671; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-366017, EBI-5235340;
CC Q13671; O75886: STAM2; NbExp=4; IntAct=EBI-366017, EBI-373258;
CC Q13671; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-366017, EBI-1644036;
CC Q13671; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-366017, EBI-1105213;
CC Q13671; Q12933: TRAF2; NbExp=3; IntAct=EBI-366017, EBI-355744;
CC Q13671; P36406: TRIM23; NbExp=3; IntAct=EBI-366017, EBI-740098;
CC Q13671; P14373: TRIM27; NbExp=3; IntAct=EBI-366017, EBI-719493;
CC Q13671; Q9C029: TRIM7; NbExp=3; IntAct=EBI-366017, EBI-2813981;
CC Q13671; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-366017, EBI-6550597;
CC Q13671; Q86WV8: TSC1; NbExp=3; IntAct=EBI-366017, EBI-12806590;
CC Q13671; P62258: YWHAE; NbExp=3; IntAct=EBI-366017, EBI-356498;
CC Q13671; O96006: ZBED1; NbExp=3; IntAct=EBI-366017, EBI-740037;
CC Q13671-1; P01112: HRAS; NbExp=2; IntAct=EBI-366030, EBI-350145;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11784866}. Membrane
CC {ECO:0000269|PubMed:11784866}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11784866}. Note=Some amount is membrane-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RIN1;
CC IsoId=Q13671-1; Sequence=Displayed;
CC Name=RIN1-delta;
CC IsoId=Q13671-2; Sequence=VSP_004377;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined with high levels
CC in brain, placenta and pancreas. {ECO:0000269|PubMed:9144171}.
CC -!- PTM: Phosphorylated on tyrosine residues by ABL1 and ABL2.
CC Phosphorylation at Ser-351 by PRKD1 induces interaction with 14-3-3
CC proteins. {ECO:0000269|PubMed:11784866, ECO:0000269|PubMed:15886098,
CC ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9208849}.
CC -!- MISCELLANEOUS: [Isoform RIN1-delta]: Shows reduced ability to bind to
CC Ras and 14-3-3 proteins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC {ECO:0000305}.
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DR EMBL; L36463; AAB67270.1; -; mRNA.
DR EMBL; BC014417; AAH14417.1; -; mRNA.
DR CCDS; CCDS31614.1; -. [Q13671-1]
DR PIR; A58613; A38637.
DR RefSeq; NP_004283.2; NM_004292.2. [Q13671-1]
DR AlphaFoldDB; Q13671; -.
DR SMR; Q13671; -.
DR BioGRID; 114972; 148.
DR CORUM; Q13671; -.
DR DIP; DIP-117N; -.
DR IntAct; Q13671; 67.
DR MINT; Q13671; -.
DR STRING; 9606.ENSP00000310406; -.
DR iPTMnet; Q13671; -.
DR PhosphoSitePlus; Q13671; -.
DR BioMuta; RIN1; -.
DR DMDM; 116242760; -.
DR EPD; Q13671; -.
DR jPOST; Q13671; -.
DR MassIVE; Q13671; -.
DR MaxQB; Q13671; -.
DR PaxDb; Q13671; -.
DR PeptideAtlas; Q13671; -.
DR PRIDE; Q13671; -.
DR ProteomicsDB; 59652; -. [Q13671-1]
DR ProteomicsDB; 59653; -. [Q13671-2]
DR Antibodypedia; 30128; 213 antibodies from 30 providers.
DR DNASU; 9610; -.
DR Ensembl; ENST00000311320.9; ENSP00000310406.4; ENSG00000174791.11. [Q13671-1]
DR GeneID; 9610; -.
DR KEGG; hsa:9610; -.
DR MANE-Select; ENST00000311320.9; ENSP00000310406.4; NM_004292.3; NP_004283.2.
DR UCSC; uc001ohn.2; human. [Q13671-1]
DR CTD; 9610; -.
DR DisGeNET; 9610; -.
DR GeneCards; RIN1; -.
DR HGNC; HGNC:18749; RIN1.
DR HPA; ENSG00000174791; Tissue enhanced (esophagus, skin).
DR MIM; 605965; gene.
DR neXtProt; NX_Q13671; -.
DR OpenTargets; ENSG00000174791; -.
DR PharmGKB; PA38671; -.
DR VEuPathDB; HostDB:ENSG00000174791; -.
DR eggNOG; KOG2320; Eukaryota.
DR GeneTree; ENSGT00940000161834; -.
DR InParanoid; Q13671; -.
DR OMA; WPETQEA; -.
DR PhylomeDB; Q13671; -.
DR TreeFam; TF331067; -.
DR PathwayCommons; Q13671; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q13671; -.
DR SIGNOR; Q13671; -.
DR BioGRID-ORCS; 9610; 15 hits in 1073 CRISPR screens.
DR ChiTaRS; RIN1; human.
DR GeneWiki; RIN1; -.
DR GenomeRNAi; 9610; -.
DR Pharos; Q13671; Tbio.
DR PRO; PR:Q13671; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13671; protein.
DR Bgee; ENSG00000174791; Expressed in parotid gland and 197 other tissues.
DR ExpressionAtlas; Q13671; baseline and differential.
DR Genevisible; Q13671; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Endocytosis;
KW GTPase activation; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..783
FT /note="Ras and Rab interactor 1"
FT /id="PRO_0000191317"
FT DOMAIN 69..163
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 456..598
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT DOMAIN 624..706
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..727
FT /note="Ras and 14-3-3 protein binding region"
FT REGION 295..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 36
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000269|PubMed:15886098"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 351
FT /note="Phosphoserine; by PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:11784866,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 692
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 429..490
FT /note="Missing (in isoform RIN1-delta)"
FT /evidence="ECO:0000303|PubMed:9144171"
FT /id="VSP_004377"
FT MUTAGEN 351
FT /note="S->A: Abolishes phosphorylation by PKD and the
FT interaction with 14-3-3 proteins."
FT /evidence="ECO:0000269|PubMed:11784866"
FT CONFLICT 392..395
FT /note="AGPE -> DGQR (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="Q -> E (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="L -> V (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="L -> V (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="A -> S (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="E -> G (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 84099 MW; 2B4DA70147CDDDFE CRC64;
MESPGESGAG SPGAPSPSSF TTGHLAREKP AQDPLYDVPN ASGGQAGGPQ RPGRVVSLRE
RLLLTRPVWL QLQANAAAAL HMLRTEPPGT FLVRKSNTRQ CQALCMRLPE ASGPSFVSSH
YILESPGGVS LEGSELMFPD LVQLICAYCH TRDILLLPLQ LPRAIHHAAT HKELEAISHL
GIEFWSSSLN IKAQRGPAGG PVLPQLKARS PQELDQGTGA ALCFFNPLFP GDLGPTKREK
FKRSFKVRVS TETSSPLSPP AVPPPPVPVL PGAVPSQTER LPPCQLLRRE SSVGYRVPAG
SGPSLPPMPS LQEVDCGSPS SSEEEGVPGS RGSPATSPHL GRRRPLLRSM SAAFCSLLAP
ERQVGRAAAA LMQDRHTAAG QLVQDLLTQV RAGPEPQELQ GIRQALSRAR AMLSAELGPE
KLLSPKRLEH VLEKSLHCSV LKPLRPILAA RLRRRLAADG SLGRLAEGLR LARAQGPGAF
GSHLSLPSPV ELEQVRQKLL QLLRTYSPSA QVKRLLQACK LLYMALRTQE GEGAGADEFL
PLLSLVLAHC DLPELLLEAE YMSELLEPSL LTGEGGYYLT SLSASLALLS GLGQAHTLPL
SPVQELRRSL SLWEQRRLPA THCFQHLLRV AYQDPSSGCT SKTLAVPPEA SIATLNQLCA
TKFRVTQPNT FGLFLYKEQG YHRLPPGALA HRLPTTGYLV YRRAEWPETQ GAVTEEEGSG
QSEARSRGEE QGCQGDGDAG VKASPRDIRE QSETTAEGGQ GQAQEGPAQP GEPEAEGSRA
AEE
