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 24-JAN-2024, entry version 208. 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 PERRS1 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 1 (PERRS1) CC [MIM:608415]: A form of bradyopsia, an ocular disorder characterized by CC prolonged electroretinal response suppression leading to difficulties CC adjusting to changes in luminance, normal to subnormal acuity and CC photophobia. PERRS1 is an autosomal recessive form with onset in CC childhood. {ECO:0000269|PubMed:14702087}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAC25430.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-31365; -. DR EMDB; EMD-31366; -. DR SMR; O75916; -. DR BioGRID; 114315; 13. 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; 9606-ENSP00000262406; -. DR PeptideAtlas; 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; 183 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 AGR; HGNC:10004; -. DR CTD; 8787; -. DR DisGeNET; 8787; -. DR GeneCards; RGS9; -. DR HGNC; HGNC:10004; RGS9. DR HPA; ENSG00000108370; Tissue enriched (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; PRMACLR; -. DR OrthoDB; 22856at2759; -. 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 1151 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 105 other cell types or tissues. DR ExpressionAtlas; O75916; baseline and differential. 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:0042734; C:presynaptic 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:0007212; P:dopamine receptor signaling pathway; 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:0007399; P:nervous system development; IEA:Ensembl. DR GO; GO:1905912; P:regulation of calcium ion export across plasma membrane; IEA:Ensembl. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd04450; DEP_RGS7-like; 1. DR CDD; cd00068; GGL; 1. DR CDD; cd08739; RGS_RGS9; 1. DR Gene3D; 1.10.1240.60; -; 1. DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1. DR Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR047016; RGS6/7/9/11. DR InterPro; IPR047017; RGS6/7/9/11_DHEX_sf. DR InterPro; IPR047077; RGS9_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 PANTHER; PTHR45746; LP21163P; 1. DR PANTHER; PTHR45746:SF1; REGULATOR OF G-PROTEIN SIGNALING 9; 1. 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; SM01224; G_gamma; 1. DR SMART; SM00224; GGL; 1. DR SMART; SM00315; RGS; 1. DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1. DR SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS50132; RGS; 1. DR Genevisible; O75916; HS. 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 PERRS1; 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 //