RGS9_HUMAN
ID RGS9_HUMAN Reviewed; 674 AA.
AC O75916; A8K3C0; O75573; Q696R2; Q8TD64; Q8TD65; Q9HC32; Q9HC33;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Regulator of G-protein signaling 9;
DE Short=RGS9;
GN Name=RGS9;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Retina;
RX PubMed=9765512;
RA Granneman J.G., Zhai Y., Zhu Z., Bannon M.J., Burchett S.A., Schmidt C.J.,
RA Andrade R., Cooper J.;
RT "Molecular characterization of human and rat RGS9L, a novel splice variant
RT enriched in dopamine target regions, and chromosomal localization of the
RT RGS9 gene.";
RL Mol. Pharmacol. 54:687-694(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 3 AND
RP 5).
RX PubMed=10564809; DOI=10.1016/s0378-1119(99)00393-5;
RA Zhang K., Howes K.A., He W., Pettenati M.J., Palczewski K., Wensel T.G.,
RA Baehr W.;
RT "Structure, alternative splicing, and expression of the human RGS9 gene.";
RL Gene 240:23-34(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-674 (ISOFORM 1).
RA Chatterjee T.K., Fisher R.A.;
RT "Homo sapiens regulator of G protein signaling 9.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP DEP DOMAIN TARGETING FUNCTION.
RX PubMed=14614075; DOI=10.1523/jneurosci.23-32-10175.2003;
RA Martemyanov K.A., Lishko P.V., Calero N., Keresztes G., Sokolov M.,
RA Strissel K.J., Leskov I.B., Hopp J.A., Kolesnikov A.V., Chen C.-K., Lem J.,
RA Heller S., Burns M.E., Arshavsky V.Y.;
RT "The DEP domain determines subcellular targeting of the GTPase activating
RT protein RGS9 in vivo.";
RL J. Neurosci. 23:10175-10181(2003).
RN [9]
RP VARIANT PERRS ARG-299.
RX PubMed=14702087; DOI=10.1038/nature02170;
RA Nishiguchi K.M., Sandberg M.A., Kooijman A.C., Martemyanov K.A.,
RA Pott J.W.R., Hagstrom S.A., Arshavsky V.Y., Berson E.L., Dryja T.P.;
RT "Defects in RGS9 or its anchor protein R9AP in patients with slow
RT photoreceptor deactivation.";
RL Nature 427:75-78(2004).
CC -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC activity of G protein alpha subunits thereby driving them into their
CC inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction;
CC key element in the recovery phase of visual transduction (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with GNB5. Interacts with RGS7BP, leading to
CC regulate the subcellular location of the heterodimer formed with GNB5.
CC Component of the RGS9-1-Gbeta5 complex composed of RGS9 (RGS9-1),
CC Gbeta5 (GNB5) and RGS9BP. Interacts with PDE6G and GNAT1.
CC {ECO:0000250|UniProtKB:O46469}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Membrane; Peripheral membrane
CC protein. Note=Isoform 3 is targeted to the membrane via its interaction
CC with RGS9BP. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=RGS9L;
CC IsoId=O75916-1; Sequence=Displayed;
CC Name=2; Synonyms=RGS9S;
CC IsoId=O75916-2; Sequence=VSP_005675;
CC Name=3; Synonyms=RGS9-1;
CC IsoId=O75916-3; Sequence=VSP_038381, VSP_038382, VSP_038383;
CC Name=4;
CC IsoId=O75916-4; Sequence=VSP_005674;
CC Name=5;
CC IsoId=O75916-5; Sequence=VSP_038381;
CC -!- TISSUE SPECIFICITY: Highly expressed in the caudate and putamen, lower
CC levels found in the hypothalamus and nucleus accumbens and very low
CC levels in cerebellum. Not expressed in globus pallidus or cingulate
CC cortex. Isoform 2 is expressed predominantly in pineal gland and
CC retina. Isoform 3 is expressed in retina (abundant in photoreceptors).
CC -!- DOMAIN: In photoreceptor cells the DEP domain is essential for
CC targeting RGS9 to the outer rod segments.
CC {ECO:0000269|PubMed:14614075}.
CC -!- PTM: Retinal isoform 3 is light-dependent phosphorylated at 'Ser-478'.
CC Phosphorylation is decreased by light exposition (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Prolonged electroretinal response suppression (PERRS)
CC [MIM:608415]: Characterized by difficulty adjusting to sudden changes
CC in luminance levels mediated by cones. {ECO:0000269|PubMed:14702087}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25430.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF071476; AAC64040.1; -; mRNA.
DR EMBL; AF178070; AAG09311.1; -; Genomic_DNA.
DR EMBL; AF178056; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178057; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178058; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178059; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178060; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178061; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178062; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178063; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178064; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178065; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178066; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178067; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178068; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178069; AAG09311.1; JOINED; Genomic_DNA.
DR EMBL; AF178072; AAG09312.1; -; Genomic_DNA.
DR EMBL; AF178056; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178057; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178058; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178059; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178060; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178061; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178062; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178063; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178064; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178065; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178066; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178067; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178068; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178069; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178070; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF178071; AAG09312.1; JOINED; Genomic_DNA.
DR EMBL; AF493932; AAM12646.1; -; mRNA.
DR EMBL; AF493933; AAM12647.1; -; mRNA.
DR EMBL; AY585190; AAT79493.1; -; mRNA.
DR EMBL; AY585191; AAT79494.1; -; mRNA.
DR EMBL; AK290535; BAF83224.1; -; mRNA.
DR EMBL; AC015821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC060771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW88998.1; -; Genomic_DNA.
DR EMBL; AF073710; AAC25430.1; ALT_INIT; mRNA.
DR CCDS; CCDS42373.1; -. [O75916-1]
DR CCDS; CCDS45764.1; -. [O75916-5]
DR RefSeq; NP_001075424.1; NM_001081955.2. [O75916-5]
DR RefSeq; NP_003826.2; NM_003835.3. [O75916-1]
DR AlphaFoldDB; O75916; -.
DR SMR; O75916; -.
DR BioGRID; 114315; 12.
DR IntAct; O75916; 6.
DR MINT; O75916; -.
DR STRING; 9606.ENSP00000262406; -.
DR iPTMnet; O75916; -.
DR PhosphoSitePlus; O75916; -.
DR BioMuta; RGS9; -.
DR EPD; O75916; -.
DR MassIVE; O75916; -.
DR PaxDb; O75916; -.
DR PeptideAtlas; O75916; -.
DR PRIDE; O75916; -.
DR ProteomicsDB; 50271; -. [O75916-1]
DR ProteomicsDB; 50272; -. [O75916-2]
DR ProteomicsDB; 50273; -. [O75916-3]
DR ProteomicsDB; 50274; -. [O75916-4]
DR ProteomicsDB; 50275; -. [O75916-5]
DR Antibodypedia; 9570; 170 antibodies from 29 providers.
DR DNASU; 8787; -.
DR Ensembl; ENST00000262406.10; ENSP00000262406.9; ENSG00000108370.17. [O75916-1]
DR Ensembl; ENST00000449996.7; ENSP00000396329.3; ENSG00000108370.17. [O75916-5]
DR GeneID; 8787; -.
DR KEGG; hsa:8787; -.
DR MANE-Select; ENST00000262406.10; ENSP00000262406.9; NM_003835.4; NP_003826.2.
DR UCSC; uc002jfd.4; human. [O75916-1]
DR CTD; 8787; -.
DR DisGeNET; 8787; -.
DR GeneCards; RGS9; -.
DR HGNC; HGNC:10004; RGS9.
DR HPA; ENSG00000108370; Tissue enhanced (brain).
DR MalaCards; RGS9; -.
DR MIM; 604067; gene.
DR MIM; 608415; phenotype.
DR neXtProt; NX_O75916; -.
DR OpenTargets; ENSG00000108370; -.
DR Orphanet; 75374; Bradyopsia.
DR PharmGKB; PA34380; -.
DR VEuPathDB; HostDB:ENSG00000108370; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000156505; -.
DR InParanoid; O75916; -.
DR OMA; TNVDITQ; -.
DR PhylomeDB; O75916; -.
DR TreeFam; TF351956; -.
DR PathwayCommons; O75916; -.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade. [O75916-3]
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; O75916; -.
DR BioGRID-ORCS; 8787; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; RGS9; human.
DR GeneWiki; RGS9; -.
DR GenomeRNAi; 8787; -.
DR Pharos; O75916; Tbio.
DR PRO; PR:O75916; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75916; protein.
DR Bgee; ENSG00000108370; Expressed in putamen and 104 other tissues.
DR ExpressionAtlas; O75916; baseline and differential.
DR Genevisible; O75916; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:1990603; P:dark adaptation; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0036367; P:light adaption; IEA:Ensembl.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR040759; RGS_DHEX.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00631; G-gamma; 1.
DR Pfam; PF00615; RGS; 1.
DR Pfam; PF18148; RGS_DHEX; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00224; GGL; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Membrane; Phosphoprotein;
KW Reference proteome; Sensory transduction; Signal transduction inhibitor;
KW Vision.
FT CHAIN 1..674
FT /note="Regulator of G-protein signaling 9"
FT /id="PRO_0000204203"
FT DOMAIN 30..105
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 219..280
FT /note="G protein gamma"
FT DOMAIN 298..413
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 533..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005674"
FT VAR_SEQ 216..218
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_038381"
FT VAR_SEQ 470..674
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9765512"
FT /id="VSP_005675"
FT VAR_SEQ 470..487
FT /note="PGQHMAPSPHLTVYTGTC -> VMSKLDRRSQLKKELPPK (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038382"
FT VAR_SEQ 488..674
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038383"
FT VARIANT 258
FT /note="S -> L (in dbSNP:rs12452285)"
FT /id="VAR_051796"
FT VARIANT 299
FT /note="W -> R (in PERRS; dbSNP:rs121908449)"
FT /evidence="ECO:0000269|PubMed:14702087"
FT /id="VAR_017912"
FT CONFLICT 112
FT /note="Q -> R (in Ref. 2; AAG09311/AAG09312)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="E -> G (in Ref. 3; AAM12647)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> S (in Ref. 3; AAM12646)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="F -> S (in Ref. 3; AAM12647)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="E -> G (in Ref. 3; AAM12647)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="Q -> R (in Ref. 3; AAM12647)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="L -> Q (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="E -> D (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="K -> R (in Ref. 3; AAM12647)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="E -> G (in Ref. 3; AAM12646)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="E -> K (in Ref. 2; AAG09311/AAG09312)"
FT /evidence="ECO:0000305"
FT CONFLICT 518..519
FT /note="Missing (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 527..531
FT /note="RVALE -> LVVLD (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 544..549
FT /note="GSMAPR -> WSGANP (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="E -> D (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="L -> R (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="S -> P (in Ref. 3; AAM12647)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="P -> T (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="P -> L (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="L -> V (in Ref. 7; AAC25430)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="I -> T (in Ref. 3; AAM12646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 674 AA; 76966 MW; 8E2B11104B448364 CRC64;
MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMQNQR VLVTSVPHAM TGSDVLQWIV
QRLWISSLEA QNLGNFIVRY GYIYPLQDPK NLILKPDGSL YRFQTPYFWP TQQWPAEDTD
YAIYLAKRNI KKKGILEEYE KENYNFLNQK MNYKWDFVIM QAKEQYRAGK ERNKADRYAL
DCQEKAYWLV HRCPPGMDNV LDYGLDRVTN PNEVKVNQKQ TVVAVKKEIM YYQQALMRST
VKSSVSLGGI VKYSEQFSSN DAIMSGCLPS NPWITDDTQF WDLNAKLVEI PTKMRVERWA
FNFSELIRDP KGRQSFQYFL KKEFSGENLG FWEACEDLKY GDQSKVKEKA EEIYKLFLAP
GARRWINIDG KTMDITVKGL KHPHRYVLDA AQTHIYMLMK KDSYARYLKS PIYKDMLAKA
IEPQETTKKS STLPFMRRHL RSSPSPVILR QLEEEAKARE AANTVDITQP GQHMAPSPHL
TVYTGTCMPP SPSSPFSSSC RSPRKPFASP SRFIRRPSTT ICPSPIRVAL ESSSGLEQKG
ECSGSMAPRG PSVTESSEAS LDTSWPRSRP RAPPKARMAL SFSRFLRRGC LASPVFARLS
PKCPAVSHGR VQPLGDVGQQ LPRLKSKRVA NFFQIKMDVP TGSGTCLMDS EDAGTGESGD
RATEKEVICP WESL
