ID   RGS20_HUMAN             Reviewed;         388 AA.
AC   O76081; Q96BG9;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 4.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=Regulator of G-protein signaling 20;
DE            Short=RGS20;
DE   AltName: Full=Gz-selective GTPase-activating protein;
DE            Short=G(z)GAP;
DE            Short=Gz-GAP;
DE   AltName: Full=Regulator of G-protein signaling Z1;
DE   AltName: Full=Regulator of Gz-selective protein signaling 1;
GN   Name=RGS20; Synonyms=RGSZ1, ZGAP1;
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 5), AND CHARACTERIZATION.
RC   TISSUE=Fetal brain;
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   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Wang J., Ducret A., Ross E.M.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 6).
RC   TISSUE=Retina;
RX   PubMed=11735229; DOI=10.1006/geno.2001.6659;
RA   Barker S.A., Wang J., Sierra D.A., Ross E.M.;
RT   "RGSZ1 and Ret RGS: two of several splice variants from the gene RGS20.";
RL   Genomics 78:223-229(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Fetal brain, and Skin;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 57-388 (ISOFORM 1).
RX   PubMed=9748279; DOI=10.1074/jbc.273.40.26008;
RA   Glick J.L., Meigs T.E., Miron A., Casey P.J.;
RT   "RGSZ1, a Gz-selective regulator of G protein signaling whose action is
RT   sensitive to the phosphorylation state of Gzalpha.";
RL   J. Biol. Chem. 273:26008-26013(1998).
RN   [7]
RP   FUNCTION.
RX   PubMed=12379657; DOI=10.1074/jbc.m206116200;
RA   Wang Y., Ho G., Zhang J.J., Nieuwenhuijsen B., Edris W., Chanda P.K.,
RA   Young K.H.;
RT   "Regulator of G protein signaling Z1 (RGSZ1) interacts with Galpha i
RT   subunits and regulates Galpha i-mediated cell signaling.";
RL   J. Biol. Chem. 277:48325-48332(2002).
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 selectively to G(z)-alpha and G(alpha)-
CC       i2 subunits, accelerates their GTPase activity and regulates their
CC       signaling activities. The G(z)-alpha activity is inhibited by the
CC       phosphorylation and palmitoylation of the G-protein. Negatively
CC       regulates mu-opioid receptor-mediated activation of the G-proteins (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:12379657}.
CC   -!- SUBUNIT: Forms a complex with G(alpha)z/i2 subunits and mu-opioid
CC       receptors; the formation of this complex results in mu-opioid receptor
CC       desensitization. Interacts with OPRM1 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       O76081; P29972: AQP1; NbExp=3; IntAct=EBI-1052678, EBI-745213;
CC       O76081; Q8NEC5: CATSPER1; NbExp=4; IntAct=EBI-1052678, EBI-744545;
CC       O76081; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-1052678, EBI-713677;
CC       O76081; Q02930-3: CREB5; NbExp=3; IntAct=EBI-1052678, EBI-10192698;
CC       O76081; P48023: FASLG; NbExp=3; IntAct=EBI-1052678, EBI-495538;
CC       O76081; O76003: GLRX3; NbExp=4; IntAct=EBI-1052678, EBI-374781;
CC       O76081; P49639: HOXA1; NbExp=5; IntAct=EBI-1052678, EBI-740785;
CC       O76081; P10809: HSPD1; NbExp=3; IntAct=EBI-1052678, EBI-352528;
CC       O76081; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-1052678, EBI-6426443;
CC       O76081; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-1052678, EBI-10172511;
CC       O76081; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-1052678, EBI-3958099;
CC       O76081; Q5T7P3: LCE1B; NbExp=5; IntAct=EBI-1052678, EBI-10245913;
CC       O76081; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-1052678, EBI-10246750;
CC       O76081; Q5T5B0: LCE3E; NbExp=3; IntAct=EBI-1052678, EBI-10245456;
CC       O76081; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-1052678, EBI-10246358;
CC       O76081; O60336: MAPKBP1; NbExp=3; IntAct=EBI-1052678, EBI-947402;
CC       O76081; P48039: MTNR1A; NbExp=6; IntAct=EBI-1052678, EBI-1188238;
CC       O76081; P49286: MTNR1B; NbExp=2; IntAct=EBI-1052678, EBI-1188341;
CC       O76081; Q9NQS3: NECTIN3; NbExp=3; IntAct=EBI-1052678, EBI-2826725;
CC       O76081; P32242: OTX1; NbExp=5; IntAct=EBI-1052678, EBI-740446;
CC       O76081; P43115-12: PTGER3; NbExp=3; IntAct=EBI-1052678, EBI-10234038;
CC       O76081; Q9NWL9; NbExp=3; IntAct=EBI-1052678, EBI-10315054;
CC       O76081; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-1052678, EBI-3957603;
CC       O76081-6; P05187: ALPP; NbExp=3; IntAct=EBI-10178530, EBI-1211484;
CC       O76081-6; P29972: AQP1; NbExp=3; IntAct=EBI-10178530, EBI-745213;
CC       O76081-6; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-10178530, EBI-744545;
CC       O76081-6; P27658: COL8A1; NbExp=3; IntAct=EBI-10178530, EBI-747133;
CC       O76081-6; Q9UGL9: CRCT1; NbExp=6; IntAct=EBI-10178530, EBI-713677;
CC       O76081-6; Q02930-3: CREB5; NbExp=6; IntAct=EBI-10178530, EBI-10192698;
CC       O76081-6; P48023: FASLG; NbExp=6; IntAct=EBI-10178530, EBI-495538;
CC       O76081-6; O76003: GLRX3; NbExp=3; IntAct=EBI-10178530, EBI-374781;
CC       O76081-6; P04899: GNAI2; NbExp=3; IntAct=EBI-10178530, EBI-353997;
CC       O76081-6; P49639: HOXA1; NbExp=3; IntAct=EBI-10178530, EBI-740785;
CC       O76081-6; P04196: HRG; NbExp=3; IntAct=EBI-10178530, EBI-3915012;
CC       O76081-6; P10809: HSPD1; NbExp=3; IntAct=EBI-10178530, EBI-352528;
CC       O76081-6; I3WAC9: INS; NbExp=3; IntAct=EBI-10178530, EBI-10178524;
CC       O76081-6; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-10178530, EBI-6426443;
CC       O76081-6; Q9BYR5: KRTAP4-2; NbExp=6; IntAct=EBI-10178530, EBI-10172511;
CC       O76081-6; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-10178530, EBI-11993296;
CC       O76081-6; Q6L8G9: KRTAP5-6; NbExp=6; IntAct=EBI-10178530, EBI-10250562;
CC       O76081-6; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-10178530, EBI-3958099;
CC       O76081-6; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-10178530, EBI-1043191;
CC       O76081-6; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-10178530, EBI-11958364;
CC       O76081-6; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-10178530, EBI-11962058;
CC       O76081-6; Q5T7P3: LCE1B; NbExp=6; IntAct=EBI-10178530, EBI-10245913;
CC       O76081-6; Q5T754: LCE1F; NbExp=3; IntAct=EBI-10178530, EBI-11958008;
CC       O76081-6; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-10178530, EBI-10246607;
CC       O76081-6; O14633: LCE2B; NbExp=3; IntAct=EBI-10178530, EBI-11478468;
CC       O76081-6; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-10178530, EBI-11973993;
CC       O76081-6; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-10178530, EBI-9394625;
CC       O76081-6; Q5T5A8: LCE3C; NbExp=3; IntAct=EBI-10178530, EBI-10245291;
CC       O76081-6; Q9BYE3: LCE3D; NbExp=3; IntAct=EBI-10178530, EBI-6658837;
CC       O76081-6; Q5T5B0: LCE3E; NbExp=6; IntAct=EBI-10178530, EBI-10245456;
CC       O76081-6; Q5TA78: LCE4A; NbExp=8; IntAct=EBI-10178530, EBI-10246358;
CC       O76081-6; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-10178530, EBI-11955689;
CC       O76081-6; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10178530, EBI-739832;
CC       O76081-6; O60336: MAPKBP1; NbExp=3; IntAct=EBI-10178530, EBI-947402;
CC       O76081-6; Q92692-2: NECTIN2; NbExp=3; IntAct=EBI-10178530, EBI-6979889;
CC       O76081-6; Q86SG6: NEK8; NbExp=3; IntAct=EBI-10178530, EBI-1752987;
CC       O76081-6; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-10178530, EBI-1210753;
CC       O76081-6; P32242: OTX1; NbExp=3; IntAct=EBI-10178530, EBI-740446;
CC       O76081-6; P43115-12: PTGER3; NbExp=3; IntAct=EBI-10178530, EBI-10234038;
CC       O76081-6; Q8WUK0: PTPMT1; NbExp=6; IntAct=EBI-10178530, EBI-7199479;
CC       O76081-6; Q6EMK4: VASN; NbExp=3; IntAct=EBI-10178530, EBI-10249550;
CC       O76081-6; A0A384ME25; NbExp=3; IntAct=EBI-10178530, EBI-10211777;
CC       O76081-6; Q9NWL9; NbExp=3; IntAct=EBI-10178530, EBI-10315054;
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm.
CC       Note=Shuttles between the cytoplasm/cell membrane and the nucleus.
CC       Anchored to the membrane through palmitoylation. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=6;
CC         IsoId=O76081-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=O76081-2; Sequence=VSP_005696;
CC       Name=2;
CC         IsoId=O76081-3; Sequence=VSP_005697, VSP_005699;
CC       Name=3;
CC         IsoId=O76081-4; Sequence=VSP_005698, VSP_005700;
CC       Name=4;
CC         IsoId=O76081-5; Sequence=VSP_005695, VSP_005696;
CC       Name=5;
CC         IsoId=O76081-6; Sequence=VSP_005694, VSP_005696;
CC   -!- TISSUE SPECIFICITY: Isoform 5 is expressed in brain at high levels in
CC       the caudate nucleus and temporal lobe.
CC   -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: N- and O-glycosylated in synapsomal membranes. {ECO:0000250}.
CC   -!- PTM: Serine phosphorylated in synapsomal membranes. {ECO:0000250}.
CC   -!- PTM: Sumoylated with SUMO1 and SUMO2 in synaptosomes. The sumoylated
CC       forms act as a scaffold for sequestering mu-opioid receptor-activated
CC       G(alpha) subunits (By similarity). {ECO:0000250}.
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; AF060877; AAC62009.2; -; mRNA.
DR   EMBL; AF366054; AAK54122.1; -; mRNA.
DR   EMBL; AF366055; AAK54123.1; -; mRNA.
DR   EMBL; AF366056; AAK54124.1; -; mRNA.
DR   EMBL; AF366057; AAK54125.1; -; mRNA.
DR   EMBL; AF074979; AAC62013.1; -; mRNA.
DR   EMBL; AF493940; AAM12654.1; -; mRNA.
DR   EMBL; BC015614; AAH15614.2; -; mRNA.
DR   EMBL; BC063490; AAH63490.1; -; mRNA.
DR   EMBL; AY046538; AAL03971.1; -; mRNA.
DR   CCDS; CCDS6155.1; -. [O76081-1]
DR   CCDS; CCDS6156.1; -. [O76081-6]
DR   CCDS; CCDS69482.1; -. [O76081-2]
DR   RefSeq; NP_001273602.1; NM_001286673.1. [O76081-2]
DR   RefSeq; NP_001273603.1; NM_001286674.1. [O76081-4]
DR   RefSeq; NP_001273604.1; NM_001286675.1. [O76081-3]
DR   RefSeq; NP_003693.2; NM_003702.4. [O76081-6]
DR   RefSeq; NP_733466.1; NM_170587.3. [O76081-1]
DR   RefSeq; XP_011515924.1; XM_011517622.2.
DR   AlphaFoldDB; O76081; -.
DR   BMRB; O76081; -.
DR   SMR; O76081; -.
DR   BioGRID; 114161; 131.
DR   CORUM; O76081; -.
DR   IntAct; O76081; 53.
DR   MINT; O76081; -.
DR   STRING; 9606.ENSP00000297313; -.
DR   iPTMnet; O76081; -.
DR   PhosphoSitePlus; O76081; -.
DR   SwissPalm; O76081; -.
DR   BioMuta; RGS20; -.
DR   EPD; O76081; -.
DR   jPOST; O76081; -.
DR   MassIVE; O76081; -.
DR   MaxQB; O76081; -.
DR   PaxDb; 9606-ENSP00000297313; -.
DR   PeptideAtlas; O76081; -.
DR   ProteomicsDB; 50382; -. [O76081-1]
DR   ProteomicsDB; 50383; -. [O76081-2]
DR   ProteomicsDB; 50384; -. [O76081-3]
DR   ProteomicsDB; 50385; -. [O76081-4]
DR   ProteomicsDB; 50386; -. [O76081-5]
DR   ProteomicsDB; 50387; -. [O76081-6]
DR   Antibodypedia; 11664; 192 antibodies from 29 providers.
DR   DNASU; 8601; -.
DR   Ensembl; ENST00000276500.4; ENSP00000276500.4; ENSG00000147509.14. [O76081-6]
DR   Ensembl; ENST00000297313.8; ENSP00000297313.3; ENSG00000147509.14. [O76081-1]
DR   Ensembl; ENST00000344277.10; ENSP00000344630.6; ENSG00000147509.14. [O76081-2]
DR   GeneID; 8601; -.
DR   KEGG; hsa:8601; -.
DR   MANE-Select; ENST00000276500.5; ENSP00000276500.4; NM_003702.5; NP_003693.2. [O76081-6]
DR   UCSC; uc003xrp.5; human. [O76081-1]
DR   AGR; HGNC:14600; -.
DR   CTD; 8601; -.
DR   DisGeNET; 8601; -.
DR   GeneCards; RGS20; -.
DR   HGNC; HGNC:14600; RGS20.
DR   HPA; ENSG00000147509; Tissue enriched (brain).
DR   MIM; 607193; gene.
DR   neXtProt; NX_O76081; -.
DR   OpenTargets; ENSG00000147509; -.
DR   PharmGKB; PA34373; -.
DR   VEuPathDB; HostDB:ENSG00000147509; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000159123; -.
DR   HOGENOM; CLU_059863_0_0_1; -.
DR   InParanoid; O76081; -.
DR   OMA; DTPMGSE; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; O76081; -.
DR   TreeFam; TF315837; -.
DR   PathwayCommons; O76081; -.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-418597; G alpha (z) signalling events.
DR   SignaLink; O76081; -.
DR   BioGRID-ORCS; 8601; 10 hits in 1153 CRISPR screens.
DR   ChiTaRS; RGS20; human.
DR   GeneWiki; RGS20; -.
DR   GenomeRNAi; 8601; -.
DR   Pharos; O76081; Tbio.
DR   PRO; PR:O76081; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; O76081; Protein.
DR   Bgee; ENSG00000147509; Expressed in caudate nucleus and 129 other cell types or tissues.
DR   ExpressionAtlas; O76081; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IMP:CACAO.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005802; C:trans-Golgi network; IMP:CACAO.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR   GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   CDD; cd08746; RGS_RGS20; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR10845; REGULATOR OF G PROTEIN SIGNALING; 1.
DR   PANTHER; PTHR10845:SF276; REGULATOR OF G-PROTEIN SIGNALING 20; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; O76081; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Glycoprotein; Lipoprotein; Membrane;
KW   Nucleus; Palmitate; Phosphoprotein; Reference proteome;
KW   Signal transduction inhibitor; Ubl conjugation.
FT   CHAIN           1..388
FT                   /note="Regulator of G-protein signaling 20"
FT                   /id="PRO_0000204233"
FT   DOMAIN          262..378
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          138..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..236
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11735229"
FT                   /id="VSP_005698"
FT   VAR_SEQ         1..208
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11735229"
FT                   /id="VSP_005697"
FT   VAR_SEQ         1..55
FT                   /note="MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVP
FT                   DIK -> MRTADGGEPAGASSPAGRVDGGL (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9748280"
FT                   /id="VSP_005694"
FT   VAR_SEQ         3..55
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11735229, ECO:0000303|Ref.4"
FT                   /id="VSP_005695"
FT   VAR_SEQ         56..170
FT                   /note="Missing (in isoform 1, isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11735229,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9748279,
FT                   ECO:0000303|PubMed:9748280, ECO:0000303|Ref.4"
FT                   /id="VSP_005696"
FT   VAR_SEQ         209..220
FT                   /note="CFCWCCCCSCSC -> MKETSGLFLISS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11735229"
FT                   /id="VSP_005699"
FT   VAR_SEQ         237..247
FT                   /note="ELRADLPTWEE -> MKETSGLFLIS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11735229"
FT                   /id="VSP_005700"
SQ   SEQUENCE   388 AA;  43692 MW;  F44796D271F1765F CRC64;
     MPQLSQDNQE CLQKHFSRPS IWTQFLPLFR AQRYNTDIHQ ITENEGDLRA VPDIKSFPPA
     QLPDSPAAPK LFGLLSSPLS SLARFFSHLL RRPPPEAPRR RLDFSPLLPA LPAARLSRGH
     EELPGRLSLL LGAALALPGR PSGGRPLRPP HPVAKPREED ATAGQSSPMP QMGSERMEMR
     KRQMPAAQDT PGAAPGQPGA GSRGSNACCF CWCCCCSCSC LTVRNQEDQR PTIASHELRA
     DLPTWEESPA PTLEEVNAWA QSFDKLMVTP AGRNAFREFL RTEFSEENML FWMACEELKK
     EANKNIIEEK ARIIYEDYIS ILSPKEVSLD SRVREVINRN MVEPSQHIFD DAQLQIYTLM
     HRDSYPRFMN SAVYKDLLQS LSEKSIEA
//