ID   RGS19_HUMAN             Reviewed;         217 AA.
AC   P49795; A8K216; E1P5G9; Q53XN0; Q8TD60;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 210.
DE   RecName: Full=Regulator of G-protein signaling 19;
DE            Short=RGS19;
DE   AltName: Full=G-alpha-interacting protein;
DE            Short=GAIP;
GN   Name=RGS19; Synonyms=GAIP, GNAI3IP;
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].
RX   PubMed=8524874; DOI=10.1073/pnas.92.25.11916;
RA   de Vries L., Mousli M., Wurmser A., Farquhar M.G.;
RT   "GAIP, a protein that specifically interacts with the trimeric G protein G
RT   alpha i3, is a member of a protein family with a highly conserved core
RT   domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:11916-11920(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Subthalamic nucleus;
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=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Blood, Placenta, and Testis;
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   [8]
RP   PALMITOYLATION.
RX   PubMed=8986788; DOI=10.1073/pnas.93.26.15203;
RA   de Vries L., Elenko E., Hubler L., Jones T.L.Z., Farquhar M.G.;
RT   "GAIP is membrane-anchored by palmitoylation and interacts with the
RT   activated (GTP-bound) form of G alpha i subunits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:15203-15208(1996).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [10]
RP   IDENTIFICATION BY 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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [12]
RP   STRUCTURE BY NMR OF 79-206.
RX   PubMed=10452897; DOI=10.1006/jmbi.1999.2989;
RA   de Alba E., De Vries L., Farquhar M.G., Tjandra N.;
RT   "Solution structure of human GAIP (Galpha interacting protein): a regulator
RT   of G protein signaling.";
RL   J. Mol. Biol. 291:927-939(1999).
RN   [13]
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   [14]
RP   PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF SER-151.
RX   PubMed=10993892; DOI=10.1074/jbc.m006198200;
RA   Ogier-Denis E., Pattingre S., El Benna J., Codogno P.;
RT   "Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates
RT   its GTPase accelerating activity and autophagy in human colon cancer
RT   cells.";
RL   J. Biol. Chem. 275:39090-39095(2000).
RN   [15]
RP   INTERACTION WITH GNAO1.
RX   PubMed=34685729; DOI=10.3390/cells10102749;
RA   Solis G.P., Kozhanova T.V., Koval A., Zhilina S.S., Mescheryakova T.I.,
RA   Abramov A.A., Ishmuratov E.V., Bolshakova E.S., Osipova K.V.,
RA   Ayvazyan S.O., Lebon S., Kanivets I.V., Pyankov D.V., Troccaz S.,
RA   Silachev D.N., Zavadenko N.N., Prityko A.G., Katanaev V.L.;
RT   "Pediatric Encephalopathy: Clinical, Biochemical and Cellular Insights into
RT   the Role of Gln52 of GNAO1 and GNAI1 for the Dominant Disease.";
RL   Cells 10:0-0(2021).
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 G-alpha subfamily 1 members, with the
CC       order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha
CC       is inhibited by phosphorylation and palmitoylation of the G-protein.
CC   -!- SUBUNIT: Interacts with GIPC PDZ domain. Interacts with GNAO1
CC       (PubMed:34685729). {ECO:0000269|PubMed:34685729}.
CC   -!- INTERACTION:
CC       P49795; P05187: ALPP; NbExp=3; IntAct=EBI-874907, EBI-1211484;
CC       P49795; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-874907, EBI-744545;
CC       P49795; P49639: HOXA1; NbExp=3; IntAct=EBI-874907, EBI-740785;
CC       P49795; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-874907, EBI-10250562;
CC       P49795; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-874907, EBI-10246358;
CC       P49795; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-874907, EBI-1210753;
CC       P49795; P32242: OTX1; NbExp=3; IntAct=EBI-874907, EBI-740446;
CC       P49795; Q12837: POU4F2; NbExp=3; IntAct=EBI-874907, EBI-17236143;
CC       P49795; P25786: PSMA1; NbExp=3; IntAct=EBI-874907, EBI-359352;
CC       P49795; Q6EMK4: VASN; NbExp=3; IntAct=EBI-874907, EBI-10249550;
CC       P49795; P08753: Gnai3; Xeno; NbExp=4; IntAct=EBI-874907, EBI-874897;
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC   -!- TISSUE SPECIFICITY: Highest expression in lung. Placenta, liver and
CC       heart also express high levels of GAIP.
CC   -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC       motif. {ECO:0000269|PubMed:8986788}.
CC   -!- PTM: Phosphorylated, mainly on serine residues.
CC       {ECO:0000269|PubMed:10993892}.
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DR   EMBL; X91809; CAA62919.1; -; mRNA.
DR   EMBL; AF493939; AAM12653.1; -; mRNA.
DR   EMBL; AY585188; AAS94232.1; -; mRNA.
DR   EMBL; BT009804; AAP88806.1; -; mRNA.
DR   EMBL; AK290081; BAF82770.1; -; mRNA.
DR   EMBL; AL590548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75166.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75167.1; -; Genomic_DNA.
DR   EMBL; BC001318; AAH01318.1; -; mRNA.
DR   EMBL; BC054337; AAH54337.1; -; mRNA.
DR   EMBL; BC063010; AAH63010.1; -; mRNA.
DR   CCDS; CCDS13555.1; -.
DR   RefSeq; NP_001034556.1; NM_001039467.1.
DR   RefSeq; NP_005864.1; NM_005873.2.
DR   RefSeq; XP_011526787.1; XM_011528485.2.
DR   RefSeq; XP_011526788.1; XM_011528486.2.
DR   PDB; 1CMZ; NMR; -; A=79-206.
DR   PDBsum; 1CMZ; -.
DR   AlphaFoldDB; P49795; -.
DR   SMR; P49795; -.
DR   BioGRID; 115576; 29.
DR   CORUM; P49795; -.
DR   IntAct; P49795; 21.
DR   MINT; P49795; -.
DR   STRING; 9606.ENSP00000378483; -.
DR   BindingDB; P49795; -.
DR   ChEMBL; CHEMBL3707468; -.
DR   GuidetoPHARMACOLOGY; 2802; -.
DR   iPTMnet; P49795; -.
DR   PhosphoSitePlus; P49795; -.
DR   SwissPalm; P49795; -.
DR   BioMuta; RGS19; -.
DR   DMDM; 1730186; -.
DR   EPD; P49795; -.
DR   jPOST; P49795; -.
DR   MassIVE; P49795; -.
DR   MaxQB; P49795; -.
DR   PaxDb; 9606-ENSP00000378483; -.
DR   PeptideAtlas; P49795; -.
DR   ProteomicsDB; 56122; -.
DR   Pumba; P49795; -.
DR   Antibodypedia; 29985; 499 antibodies from 29 providers.
DR   DNASU; 10287; -.
DR   Ensembl; ENST00000332298.9; ENSP00000333194.5; ENSG00000171700.14.
DR   Ensembl; ENST00000395042.2; ENSP00000378483.1; ENSG00000171700.14.
DR   GeneID; 10287; -.
DR   KEGG; hsa:10287; -.
DR   MANE-Select; ENST00000395042.2; ENSP00000378483.1; NM_005873.3; NP_005864.1.
DR   UCSC; uc002yhy.4; human.
DR   AGR; HGNC:13735; -.
DR   CTD; 10287; -.
DR   DisGeNET; 10287; -.
DR   GeneCards; RGS19; -.
DR   HGNC; HGNC:13735; RGS19.
DR   HPA; ENSG00000171700; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 605071; gene.
DR   neXtProt; NX_P49795; -.
DR   OpenTargets; ENSG00000171700; -.
DR   PharmGKB; PA34370; -.
DR   VEuPathDB; HostDB:ENSG00000171700; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000160391; -.
DR   HOGENOM; CLU_059863_0_2_1; -.
DR   InParanoid; P49795; -.
DR   OMA; MSQHETS; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; P49795; -.
DR   TreeFam; TF315837; -.
DR   PathwayCommons; P49795; -.
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; P49795; -.
DR   SIGNOR; P49795; -.
DR   BioGRID-ORCS; 10287; 13 hits in 1155 CRISPR screens.
DR   EvolutionaryTrace; P49795; -.
DR   GeneWiki; RGS19; -.
DR   GenomeRNAi; 10287; -.
DR   Pharos; P49795; Tchem.
DR   PRO; PR:P49795; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P49795; Protein.
DR   Bgee; ENSG00000171700; Expressed in granulocyte and 195 other cell types or tissues.
DR   GO; GO:0005903; C:brush border; IEA:Ensembl.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR   GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
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:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR   CDD; cd08745; RGS_RGS19; 1.
DR   Gene3D; 1.10.196.10; -; 2.
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; IPR024066; RGS_subdom1/3.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR10845; REGULATOR OF G PROTEIN SIGNALING; 1.
DR   PANTHER; PTHR10845:SF145; REGULATOR OF G-PROTEIN SIGNALING 19; 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; P49795; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Autophagy; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..217
FT                   /note="Regulator of G-protein signaling 19"
FT                   /id="PRO_0000204229"
FT   DOMAIN          90..206
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..217
FT                   /note="Interaction with GIPC"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70521"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976"
FT   MOD_RES         151
FT                   /note="Phosphoserine; by MAPK1 and MAPK3"
FT                   /evidence="ECO:0000269|PubMed:10993892"
FT   MUTAGEN         151
FT                   /note="S->A: Diminishes gap activity towards G(i)-alpha3
FT                   and autophagy in colon cancer cells."
FT                   /evidence="ECO:0000269|PubMed:10993892"
FT   CONFLICT        204
FT                   /note="A -> V (in Ref. 2; AAM12653)"
FT                   /evidence="ECO:0000305"
FT   HELIX           81..87
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           98..111
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           115..125
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           133..145
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           160..168
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           178..191
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           193..196
FT                   /evidence="ECO:0007829|PDB:1CMZ"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:1CMZ"
SQ   SEQUENCE   217 AA;  24636 MW;  925A5687DC222CBD CRC64;
     MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS WNQERRRAWQ
     ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG RSVFRAFLRT EYSEENMLFW
     LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINKKMQ EPSAHTFDDA
     QLQIYTLMHR DSYPRFLSSP TYRALLLQGP SQSSSEA
//