RGS10_HUMAN
ID RGS10_HUMAN Reviewed; 181 AA.
AC O43665; A8K408; B1AMR8; Q6IAZ6; Q96GN0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Regulator of G-protein signaling 10;
DE Short=RGS10;
GN Name=RGS10;
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), FUNCTION, AND INTERACTION WITH GNAZ
RP AND GNAI3.
RX PubMed=8774883; DOI=10.1038/383175a0;
RA Hunt T.W., Fields T.A., Casey P.J., Peralta E.G.;
RT "RGS10 is a selective activator of G alpha i GTPase activity.";
RL Nature 383:175-177(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=10791963; DOI=10.1074/jbc.m002082200;
RA Chatterjee T.K., Fisher R.A.;
RT "Cytoplasmic, nuclear, and Golgi localization of RGS proteins. Evidence for
RT N-terminal and RGS domain sequences as intracellular targeting motifs.";
RL J. Biol. Chem. 275:24013-24021(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GNAI3,
RP SUBCELLULAR LOCATION (ISOFORM 1), PHOSPHORYLATION AT SER-176, AND
RP MUTAGENESIS OF SER-176.
RX PubMed=11443111; DOI=10.1074/jbc.m100960200;
RA Burgon P.G., Lee W.L., Nixon A.B., Peralta E.G., Casey P.J.;
RT "Phosphorylation and nuclear translocation of a regulator of G protein
RT signaling (RGS10).";
RL J. Biol. Chem. 276:32828-32834(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 3).
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 MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
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 [10]
RP PALMITOYLATION AT CYS-74, AND FUNCTION.
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 [11]
RP FUNCTION.
RX PubMed=9353196; DOI=10.1126/science.278.5340.1132;
RA Tu Y., Wang J., Ross E.M.;
RT "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G
RT protein alpha subunits.";
RL Science 278:1132-1135(1997).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP STRUCTURE BY NMR OF 31-166.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RGS domain of human regulator of G-protein
RT signaling 10.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 17-160 IN COMPLEX WITH GNAI3,
RP FUNCTION, AND INTERACTION WITH GNAI1 AND GNAI3.
RX PubMed=18434541; DOI=10.1073/pnas.0801508105;
RA Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
RA Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
RA Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
RT "Structural diversity in the RGS domain and its interaction with
RT heterotrimeric G protein alpha-subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades,
CC including signaling downstream of the muscarinic acetylcholine receptor
CC CHRM2. Inhibits signal transduction by increasing the GTPase activity
CC of G protein alpha subunits, thereby driving them into their inactive
CC GDP-bound form (PubMed:8774883, PubMed:10608901, PubMed:9353196,
CC PubMed:11443111, PubMed:18434541). Modulates the activity of potassium
CC channels that are activated in response to CHRM2 signaling
CC (PubMed:11443111). Activity on GNAZ is inhibited by palmitoylation of
CC the G-protein (PubMed:9353196). {ECO:0000269|PubMed:10608901,
CC ECO:0000269|PubMed:11443111, ECO:0000269|PubMed:18434541,
CC ECO:0000269|PubMed:8774883, ECO:0000269|PubMed:9353196}.
CC -!- SUBUNIT: Interacts with GNAZ, GNAI1 and GNAI3 (PubMed:8774883,
CC PubMed:11443111, PubMed:18434541). Associates specifically with the
CC activated, GTP-bound forms of GNAZ and GNAI3 (PubMed:8774883).
CC {ECO:0000269|PubMed:11443111, ECO:0000269|PubMed:18434541,
CC ECO:0000269|PubMed:8774883}.
CC -!- INTERACTION:
CC O43665; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1057034, EBI-742388;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:11443111}. Nucleus {ECO:0000269|PubMed:11443111}.
CC Note=Forskolin treatment promotes phosphorylation and translocation to
CC the nucleus. {ECO:0000269|PubMed:11443111}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10791963}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=O43665-3; Sequence=Displayed;
CC Name=1;
CC IsoId=O43665-1; Sequence=VSP_060088;
CC Name=2;
CC IsoId=O43665-2; Sequence=VSP_060087;
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DR EMBL; AF368902; AAK52979.1; -; mRNA.
DR EMBL; AF045229; AAC03783.1; -; mRNA.
DR EMBL; AF493934; AAM12648.1; -; mRNA.
DR EMBL; AK290773; BAF83462.1; -; mRNA.
DR EMBL; CR457008; CAG33289.1; -; mRNA.
DR EMBL; AC012468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49389.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49390.1; -; Genomic_DNA.
DR EMBL; BC009361; AAH09361.1; -; mRNA.
DR CCDS; CCDS31294.1; -. [O43665-3]
DR CCDS; CCDS41572.1; -. [O43665-2]
DR PIR; S71812; S71812.
DR RefSeq; NP_001005339.1; NM_001005339.1. [O43665-3]
DR RefSeq; NP_002916.1; NM_002925.3. [O43665-2]
DR PDB; 2DLR; NMR; -; A=31-166.
DR PDB; 2I59; NMR; -; A=30-165.
DR PDB; 2IHB; X-ray; 2.71 A; B=10-160.
DR PDBsum; 2DLR; -.
DR PDBsum; 2I59; -.
DR PDBsum; 2IHB; -.
DR AlphaFoldDB; O43665; -.
DR BMRB; O43665; -.
DR SMR; O43665; -.
DR BioGRID; 111933; 13.
DR DIP; DIP-50368N; -.
DR IntAct; O43665; 2.
DR STRING; 9606.ENSP00000358099; -.
DR iPTMnet; O43665; -.
DR PhosphoSitePlus; O43665; -.
DR SwissPalm; O43665; -.
DR BioMuta; RGS10; -.
DR OGP; O43665; -.
DR EPD; O43665; -.
DR jPOST; O43665; -.
DR MassIVE; O43665; -.
DR MaxQB; O43665; -.
DR PaxDb; O43665; -.
DR PeptideAtlas; O43665; -.
DR PRIDE; O43665; -.
DR ProteomicsDB; 49096; -. [O43665-1]
DR ProteomicsDB; 49097; -. [O43665-2]
DR ProteomicsDB; 49098; -. [O43665-3]
DR TopDownProteomics; O43665-3; -. [O43665-3]
DR Antibodypedia; 3878; 225 antibodies from 31 providers.
DR DNASU; 6001; -.
DR Ensembl; ENST00000369101.7; ENSP00000358097.3; ENSG00000148908.15. [O43665-1]
DR Ensembl; ENST00000369103.3; ENSP00000358099.2; ENSG00000148908.15. [O43665-3]
DR Ensembl; ENST00000392865.5; ENSP00000376605.1; ENSG00000148908.15. [O43665-2]
DR GeneID; 6001; -.
DR KEGG; hsa:6001; -.
DR MANE-Select; ENST00000369103.3; ENSP00000358099.2; NM_001005339.2; NP_001005339.1.
DR UCSC; uc001lee.4; human. [O43665-3]
DR CTD; 6001; -.
DR DisGeNET; 6001; -.
DR GeneCards; RGS10; -.
DR HGNC; HGNC:9992; RGS10.
DR HPA; ENSG00000148908; Tissue enhanced (lymphoid).
DR MIM; 602856; gene.
DR neXtProt; NX_O43665; -.
DR OpenTargets; ENSG00000148908; -.
DR PharmGKB; PA34362; -.
DR VEuPathDB; HostDB:ENSG00000148908; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000161426; -.
DR HOGENOM; CLU_059863_1_4_1; -.
DR InParanoid; O43665; -.
DR OMA; HKKCEEQ; -.
DR OrthoDB; 275783at2759; -.
DR PhylomeDB; O43665; -.
DR TreeFam; TF315837; -.
DR PathwayCommons; O43665; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O43665; -.
DR SIGNOR; O43665; -.
DR BioGRID-ORCS; 6001; 15 hits in 1085 CRISPR screens.
DR ChiTaRS; RGS10; human.
DR EvolutionaryTrace; O43665; -.
DR GeneWiki; RGS10; -.
DR GenomeRNAi; 6001; -.
DR Pharos; O43665; Tbio.
DR PRO; PR:O43665; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O43665; protein.
DR Bgee; ENSG00000148908; Expressed in monocyte and 192 other tissues.
DR Genevisible; O43665; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IDA:UniProtKB.
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:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR CDD; cd08741; RGS_RGS10; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR037879; RGS10_RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
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 3D-structure; Alternative splicing; Cytoplasm; GTPase activation;
KW Lipoprotein; Nucleus; Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..181
FT /note="Regulator of G-protein signaling 10"
FT /id="PRO_0000204207"
FT DOMAIN 41..156
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQE5"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11443111"
FT LIPID 74
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10608901"
FT VAR_SEQ 1..17
FT /note="MFNRAVSRLSRKRPPSD -> MEH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10791963"
FT /id="VSP_060087"
FT VAR_SEQ 1..16
FT /note="MFNRAVSRLSRKRPPS -> MQSELCFA (in isoform 1)"
FT /evidence="ECO:0000269|PubMed:11443111,
FT ECO:0000269|PubMed:8774883"
FT /id="VSP_060088"
FT VARIANT 102
FT /note="A -> V (in dbSNP:rs1802228)"
FT /id="VAR_011896"
FT MUTAGEN 176
FT /note="S->A: Abolishes phosphorylation site and leads to
FT strongly reduced overall phosphorylation."
FT /evidence="ECO:0000269|PubMed:11443111"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:2IHB"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:2IHB"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:2IHB"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:2IHB"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:2IHB"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2I59"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2DLR"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:2DLR"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:2IHB"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:2IHB"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:2IHB"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2IHB"
FT TURN 154..158
FT /evidence="ECO:0007829|PDB:2I59"
SQ SEQUENCE 181 AA; 21210 MW; D83CCB98A6EE2182 CRC64;
MFNRAVSRLS RKRPPSDIHD SDGSSSSSHQ SLKSTAKWAA SLENLLEDPE GVKRFREFLK
KEFSEENVLF WLACEDFKKM QDKTQMQEKA KEIYMTFLSS KASSQVNVEG QSRLNEKILE
EPHPLMFQKL QDQIFNLMKY DSYSRFLKSD LFLKHKRTEE EEEDLPDAQT AAKRASRIYN
T
