RGS4_HUMAN
ID RGS4_HUMAN Reviewed; 205 AA.
AC P49798; A7XA56; A7XA58; A7XA59; A7YVV7; B1APZ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Regulator of G-protein signaling 4;
DE Short=RGP4;
DE Short=RGS4;
GN Name=RGS4;
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).
RX PubMed=8602223; DOI=10.1038/379742a0;
RA Druey K.M., Blumer K.J., Kang V.H., Kehrl J.H.;
RT "Inhibition of G-protein-mediated MAP kinase activation by a new mammalian
RT gene family.";
RL Nature 379:742-746(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), ALTERNATIVE SPLICING
RP (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=17707117; DOI=10.1016/j.gene.2007.07.002;
RA Ding L., Mychaleckyj J.C., Hegde A.N.;
RT "Full length cloning and expression analysis of splice variants of
RT regulator of G-protein signaling RGS4 in human and murine brain.";
RL Gene 401:46-60(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC TISSUE=Hippocampus, Thalamus, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [9]
RP PALMITOYLATION AT CYS-2; CYS-12 AND CYS-95.
RX PubMed=10608901; DOI=10.1074/jbc.274.53.38260;
RA Tu Y., Popov S., Slaughter C., Ross E.M.;
RT "Palmitoylation of a conserved cysteine in the regulator of G protein
RT signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and
RT RGS10.";
RL J. Biol. Chem. 274:38260-38267(1999).
RN [10]
RP INHIBITION.
RX PubMed=9748280; DOI=10.1074/jbc.273.40.26014;
RA Wang J., Ducret A., Tu Y., Kozasa T., Aebersold R., Ross E.M.;
RT "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane
RT association, regulation by Galphaz phosphorylation, and relationship to a
RT Gz GTPase-activating protein subfamily.";
RL J. Biol. Chem. 273:26014-26025(1998).
RN [11]
RP POSSIBLE INVOLVEMENT IN SCZD.
RX PubMed=12023979; DOI=10.1093/hmg/11.12.1373;
RA Chowdari K.V., Mirnics K., Semwal P., Wood J., Lawrence E., Bhatia T.,
RA Deshpande S.N., Thelma B.K., Ferrell R.E., Middleton F.A., Devlin B.,
RA Levitt P., Lewis D.A., Nimgaonkar V.L.;
RT "Association and linkage analyses of RGS4 polymorphisms in schizophrenia.";
RL Hum. Mol. Genet. 11:1373-1380(2002).
RN [12]
RP POSSIBLE INVOLVEMENT IN SCZD.
RX PubMed=14755443; DOI=10.1002/ajmg.b.20109;
RA Morris D.W., Rodgers A., McGhee K.A., Schwaiger S., Scully P., Quinn J.,
RA Meagher D., Waddington J.L., Gill M., Corvin A.P.;
RT "Confirming RGS4 as a susceptibility gene for schizophrenia.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 125:50-53(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. Activity on G(z)-alpha is inhibited by
CC phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-
CC alpha-1 is inhibited by palmitoylation of the G-protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=May be produced by alternative promoter usage.;
CC Name=1; Synonyms=B;
CC IsoId=P49798-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=P49798-2; Sequence=VSP_043856;
CC Name=3; Synonyms=C;
CC IsoId=P49798-3; Sequence=VSP_043853;
CC Name=4;
CC IsoId=P49798-4; Sequence=VSP_043855;
CC Name=5;
CC IsoId=P49798-5; Sequence=VSP_043854;
CC -!- TISSUE SPECIFICITY: Expressed in brain and heart. Expressed in brain at
CC protein level. Expressed in prefontal and visual cortex. Isoform 4 and
CC isoform 5 are expressed ubiquitously. Isoform 1, isoform 2 and isoform
CC 3 are not expressed in the cerebellum. {ECO:0000269|PubMed:17707117}.
CC -!- PTM: Palmitoylated on Cys-2 and/or Cys-12.
CC {ECO:0000269|PubMed:10608901}.
CC -!- PTM: Phosphorylated by cyclic GMP-dependent protein kinase.
CC {ECO:0000250}.
CC -!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial
CC psychotic disorder or group of disorders characterized by disturbances
CC in the form and content of thought (e.g. delusions, hallucinations), in
CC mood (e.g. inappropriate affect), in sense of self and relationship to
CC the external world (e.g. loss of ego boundaries, withdrawal), and in
CC behavior (e.g bizarre or apparently purposeless behavior). Although it
CC affects emotions, it is distinguished from mood disorders in which such
CC disturbances are primary. Similarly, there may be mild impairment of
CC cognitive function, and it is distinguished from the dementias in which
CC disturbed cognitive function is considered primary. Some patients
CC manifest schizophrenic as well as bipolar disorder symptoms and are
CC often given the diagnosis of schizoaffective disorder.
CC {ECO:0000269|PubMed:12023979, ECO:0000269|PubMed:14755443}.
CC Note=Disease susceptibility may be associated with variants affecting
CC the gene represented in this entry.
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DR EMBL; U27768; AAC50395.1; -; mRNA.
DR EMBL; DQ346662; ABC94590.1; -; mRNA.
DR EMBL; DQ346663; ABC94591.1; -; mRNA.
DR EMBL; DQ346664; ABC94592.1; -; mRNA.
DR EMBL; EF054877; ABL74968.1; -; mRNA.
DR EMBL; AK093959; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK295540; BAG58449.1; -; mRNA.
DR EMBL; AK296240; BAG58958.1; -; mRNA.
DR EMBL; AK312250; BAG35182.1; -; mRNA.
DR EMBL; AF493928; AAM12642.1; -; mRNA.
DR EMBL; BT007025; AAP35671.1; -; mRNA.
DR EMBL; AL583850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90727.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90728.1; -; Genomic_DNA.
DR EMBL; BC000737; AAH00737.1; -; mRNA.
DR EMBL; BC051869; AAH51869.1; -; mRNA.
DR CCDS; CCDS1243.1; -. [P49798-1]
DR CCDS; CCDS44270.1; -. [P49798-3]
DR CCDS; CCDS44271.1; -. [P49798-4]
DR CCDS; CCDS44272.1; -. [P49798-5]
DR PIR; S78221; S78221.
DR RefSeq; NP_001095915.1; NM_001102445.2. [P49798-3]
DR RefSeq; NP_001106851.1; NM_001113380.1. [P49798-5]
DR RefSeq; NP_001106852.1; NM_001113381.1. [P49798-4]
DR RefSeq; NP_005604.1; NM_005613.5. [P49798-1]
DR AlphaFoldDB; P49798; -.
DR BMRB; P49798; -.
DR SMR; P49798; -.
DR BioGRID; 111931; 18.
DR DIP; DIP-59092N; -.
DR IntAct; P49798; 5.
DR STRING; 9606.ENSP00000397181; -.
DR BindingDB; P49798; -.
DR ChEMBL; CHEMBL1795091; -.
DR GuidetoPHARMACOLOGY; 2811; -.
DR iPTMnet; P49798; -.
DR PhosphoSitePlus; P49798; -.
DR SwissPalm; P49798; -.
DR BioMuta; RGS4; -.
DR DMDM; 1710146; -.
DR jPOST; P49798; -.
DR MassIVE; P49798; -.
DR PaxDb; P49798; -.
DR PeptideAtlas; P49798; -.
DR PRIDE; P49798; -.
DR ProteomicsDB; 56129; -. [P49798-1]
DR ProteomicsDB; 56130; -. [P49798-2]
DR ProteomicsDB; 56131; -. [P49798-3]
DR ProteomicsDB; 56132; -. [P49798-4]
DR ProteomicsDB; 56133; -. [P49798-5]
DR Antibodypedia; 20521; 283 antibodies from 33 providers.
DR DNASU; 5999; -.
DR Ensembl; ENST00000367906.7; ENSP00000356882.3; ENSG00000117152.14. [P49798-5]
DR Ensembl; ENST00000367908.8; ENSP00000356884.4; ENSG00000117152.14. [P49798-4]
DR Ensembl; ENST00000367909.11; ENSP00000356885.6; ENSG00000117152.14. [P49798-1]
DR Ensembl; ENST00000421743.6; ENSP00000397181.2; ENSG00000117152.14. [P49798-3]
DR Ensembl; ENST00000527809.5; ENSP00000433261.1; ENSG00000117152.14. [P49798-5]
DR GeneID; 5999; -.
DR KEGG; hsa:5999; -.
DR MANE-Select; ENST00000367909.11; ENSP00000356885.6; NM_005613.6; NP_005604.1.
DR UCSC; uc001gcl.5; human. [P49798-1]
DR CTD; 5999; -.
DR DisGeNET; 5999; -.
DR GeneCards; RGS4; -.
DR HGNC; HGNC:10000; RGS4.
DR HPA; ENSG00000117152; Group enriched (adrenal gland, brain).
DR MIM; 181500; phenotype.
DR MIM; 602516; gene.
DR neXtProt; NX_P49798; -.
DR OpenTargets; ENSG00000117152; -.
DR PharmGKB; PA34375; -.
DR VEuPathDB; HostDB:ENSG00000117152; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000159036; -.
DR HOGENOM; CLU_059863_3_0_1; -.
DR InParanoid; P49798; -.
DR OMA; LINHECG; -.
DR OrthoDB; 1435659at2759; -.
DR PhylomeDB; P49798; -.
DR TreeFam; TF315837; -.
DR PathwayCommons; P49798; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR SignaLink; P49798; -.
DR BioGRID-ORCS; 5999; 7 hits in 1073 CRISPR screens.
DR ChiTaRS; RGS4; human.
DR GeneWiki; RGS4; -.
DR GenomeRNAi; 5999; -.
DR Pharos; P49798; Tchem.
DR PRO; PR:P49798; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P49798; protein.
DR Bgee; ENSG00000117152; Expressed in middle temporal gyrus and 164 other tissues.
DR ExpressionAtlas; P49798; baseline and differential.
DR Genevisible; P49798; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:1990791; P:dorsal root ganglion development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1900924; P:negative regulation of glycine import across plasma membrane; IEA:Ensembl.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0010460; P:positive regulation of heart rate; IEA:Ensembl.
DR GO; GO:0110053; P:regulation of actin filament organization; IEA:Ensembl.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR CDD; cd08714; RGS_RGS4; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034952; RGS4.
DR InterPro; IPR034953; RGS_RGS4.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF184; PTHR10845:SF184; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipoprotein; Palmitate; Phosphoprotein;
KW Reference proteome; Schizophrenia; Signal transduction inhibitor.
FT CHAIN 1..205
FT /note="Regulator of G-protein signaling 4"
FT /id="PRO_0000204185"
FT DOMAIN 62..178
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT LIPID 2
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10608901"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10608901"
FT LIPID 95
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10608901"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17707117"
FT /id="VSP_043854"
FT VAR_SEQ 1
FT /note="M -> MYNMMLLIQKRKGIGSQLLRAGEAEGDRGAGTAERSSDWLDGRSWAI
FT KETPTGLAGRRSEDSDNIFTGEEAKYAQSRSHSSSCRISFLLANSKLLNKM (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17707117"
FT /id="VSP_043853"
FT VAR_SEQ 72..205
FT /note="GLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQA
FT TKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLVNPSS
FT CGAEKQKGAKSSADCASLVPQCA -> EPGFLHQGRDKPEHARAYNNLL (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_043855"
FT VAR_SEQ 173
FT /note="F -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17707117"
FT /id="VSP_043856"
FT VARIANT 195
FT /note="A -> S (in dbSNP:rs14665)"
FT /id="VAR_051795"
SQ SEQUENCE 205 AA; 23256 MW; 7713F1F7496A698B CRC64;
MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHNSSHN KKDKVVICQR VSQEEVKKWA
ESLENLISHE CGLAAFKAFL KSEYSEENID FWISCEEYKK IKSPSKLSPK AKKIYNEFIS
VQATKEVNLD SCTREETSRN MLEPTITCFD EAQKKIFNLM EKDSYRRFLK SRFYLDLVNP
SSCGAEKQKG AKSSADCASL VPQCA
