COPZ1_HUMAN
ID COPZ1_HUMAN Reviewed; 177 AA.
AC P61923; B4DDX8; B4DHZ0; F8VS17; F8VWL5; Q549N6; Q9Y3C3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Coatomer subunit zeta-1;
DE AltName: Full=Zeta-1-coat protein;
DE Short=Zeta-1 COP;
GN Name=COPZ1; Synonyms=COPZ; ORFNames=CGI-120, HSPC181;
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=11056392; DOI=10.1093/oxfordjournals.jbchem.a022817;
RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
RT "Identification and characterization of novel isoforms of COP I subunits.";
RL J. Biochem. 128:793-801(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Tu Q., Yu L., Hu P.R., Zhang H.L., Huang J., Zhao S.Y.;
RT "Cloning and expression of a new human cDNA homology to B.taurus z-cop
RT mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Caudate nucleus, and Urinary bladder;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(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=Placenta;
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 PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
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 [14]
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 [15]
RP STRUCTURE BY NMR, SUBUNIT, AND MUTAGENESIS OF 58-LYS-ILE-59 AND
RP 87-GLU-LEU-88.
RX PubMed=19167404; DOI=10.1016/j.jmb.2008.12.083;
RA Yu W., Lin J., Jin C., Xia B.;
RT "Solution structure of human zeta-COP: direct evidences for structural
RT similarity between COP I and clathrin-adaptor coats.";
RL J. Mol. Biol. 386:903-912(2009).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC dilysine motifs and reversibly associates with Golgi non-clathrin-
CC coated vesicles, which further mediate biosynthetic protein transport
CC from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC complex is required for budding from Golgi membranes, and is essential
CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins
CC (By similarity). The zeta subunit may be involved in regulating the
CC coat assembly and, hence, the rate of biosynthetic protein transport
CC due to its association-dissociation properties with the coatomer
CC complex (By similarity). {ECO:0000250|UniProtKB:P53600}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000269|PubMed:19167404}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC originating from it. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P61923-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61923-2; Sequence=VSP_053675, VSP_053676;
CC Name=3;
CC IsoId=P61923-3; Sequence=VSP_055050;
CC Name=4;
CC IsoId=P61923-4; Sequence=VSP_055049;
CC Name=5;
CC IsoId=P61923-5; Sequence=VSP_055051;
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
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DR EMBL; AB047848; BAB17659.1; -; mRNA.
DR EMBL; AF151878; AAD34115.1; -; mRNA.
DR EMBL; AF161529; AAF29144.1; -; mRNA.
DR EMBL; AF086911; AAP97141.1; -; mRNA.
DR EMBL; AK293377; BAG56889.1; -; mRNA.
DR EMBL; AK295325; BAG58302.1; -; mRNA.
DR EMBL; AC078778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96774.1; -; Genomic_DNA.
DR EMBL; BC002849; AAH02849.1; -; mRNA.
DR CCDS; CCDS61137.1; -. [P61923-5]
DR CCDS; CCDS61138.1; -. [P61923-3]
DR CCDS; CCDS61139.1; -. [P61923-4]
DR CCDS; CCDS8877.1; -. [P61923-1]
DR RefSeq; NP_001258663.1; NM_001271734.1. [P61923-3]
DR RefSeq; NP_001258664.1; NM_001271735.1. [P61923-5]
DR RefSeq; NP_001258665.1; NM_001271736.1. [P61923-4]
DR RefSeq; NP_057141.1; NM_016057.2. [P61923-1]
DR PDB; 2HF6; NMR; -; A=1-149.
DR PDB; 5MC7; X-ray; 1.60 A; A/B=7-150.
DR PDBsum; 2HF6; -.
DR PDBsum; 5MC7; -.
DR AlphaFoldDB; P61923; -.
DR BMRB; P61923; -.
DR SMR; P61923; -.
DR BioGRID; 116495; 64.
DR DIP; DIP-29873N; -.
DR IntAct; P61923; 12.
DR STRING; 9606.ENSP00000449270; -.
DR GlyGen; P61923; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61923; -.
DR MetOSite; P61923; -.
DR PhosphoSitePlus; P61923; -.
DR BioMuta; COPZ1; -.
DR DMDM; 48428830; -.
DR EPD; P61923; -.
DR jPOST; P61923; -.
DR MassIVE; P61923; -.
DR MaxQB; P61923; -.
DR PaxDb; P61923; -.
DR PeptideAtlas; P61923; -.
DR PRIDE; P61923; -.
DR ProteomicsDB; 28529; -.
DR ProteomicsDB; 28992; -.
DR ProteomicsDB; 3904; -.
DR ProteomicsDB; 4260; -.
DR ProteomicsDB; 57338; -. [P61923-1]
DR TopDownProteomics; P61923-1; -. [P61923-1]
DR Antibodypedia; 27430; 226 antibodies from 25 providers.
DR DNASU; 22818; -.
DR Ensembl; ENST00000262061.7; ENSP00000262061.2; ENSG00000111481.10. [P61923-1]
DR Ensembl; ENST00000455864.6; ENSP00000410620.2; ENSG00000111481.10. [P61923-3]
DR Ensembl; ENST00000549043.5; ENSP00000449270.1; ENSG00000111481.10. [P61923-4]
DR Ensembl; ENST00000552362.5; ENSP00000448444.1; ENSG00000111481.10. [P61923-5]
DR GeneID; 22818; -.
DR KEGG; hsa:22818; -.
DR MANE-Select; ENST00000262061.7; ENSP00000262061.2; NM_016057.3; NP_057141.1.
DR UCSC; uc001sfs.3; human. [P61923-1]
DR CTD; 22818; -.
DR DisGeNET; 22818; -.
DR GeneCards; COPZ1; -.
DR HGNC; HGNC:2243; COPZ1.
DR HPA; ENSG00000111481; Low tissue specificity.
DR MIM; 615472; gene.
DR neXtProt; NX_P61923; -.
DR OpenTargets; ENSG00000111481; -.
DR PharmGKB; PA26760; -.
DR VEuPathDB; HostDB:ENSG00000111481; -.
DR eggNOG; KOG3343; Eukaryota.
DR GeneTree; ENSGT00390000004405; -.
DR HOGENOM; CLU_086803_2_0_1; -.
DR InParanoid; P61923; -.
DR OrthoDB; 1522668at2759; -.
DR PhylomeDB; P61923; -.
DR TreeFam; TF300262; -.
DR PathwayCommons; P61923; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; P61923; -.
DR BioGRID-ORCS; 22818; 739 hits in 1080 CRISPR screens.
DR ChiTaRS; COPZ1; human.
DR EvolutionaryTrace; P61923; -.
DR GeneWiki; COPZ1; -.
DR GenomeRNAi; 22818; -.
DR Pharos; P61923; Tbio.
DR PRO; PR:P61923; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P61923; protein.
DR Bgee; ENSG00000111481; Expressed in islet of Langerhans and 202 other tissues.
DR ExpressionAtlas; P61923; baseline and differential.
DR Genevisible; P61923; HS.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR039652; Coatomer_zeta.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR11043; PTHR11043; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..177
FT /note="Coatomer subunit zeta-1"
FT /id="PRO_0000193825"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..36
FT /note="MEALILEPSLYTVKAILILDNDGDRLFAKYYDDTYP -> MMEIDFLPSTMT
FT TPTPVSRSKRPLRRTFSTRPIGLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053675"
FT VAR_SEQ 1..6
FT /note="MEALIL -> MGGFRTEGMFVSLQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055049"
FT VAR_SEQ 7..29
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055050"
FT VAR_SEQ 37..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053676"
FT VAR_SEQ 147..163
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_055051"
FT MUTAGEN 58..59
FT /note="EI->KA: Reduced interaction with gamma subunit."
FT /evidence="ECO:0000269|PubMed:19167404"
FT MUTAGEN 87..88
FT /note="EL->KA: Reduced interaction with gamma subunit."
FT /evidence="ECO:0000269|PubMed:19167404"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:5MC7"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:5MC7"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5MC7"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:5MC7"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:5MC7"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5MC7"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:5MC7"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:5MC7"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5MC7"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:5MC7"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:5MC7"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:5MC7"
SQ SEQUENCE 177 AA; 20198 MW; 355530D032D3A049 CRC64;
MEALILEPSL YTVKAILILD NDGDRLFAKY YDDTYPSVKE QKAFEKNIFN KTHRTDSEIA
LLEGLTVVYK SSIDLYFYVI GSSYENELML MAVLNCLFDS LSQMLRKNVE KRALLENMEG
LFLAVDEIVD GGVILESDPQ QVVHRVALRG EDVPLTEQTV SQVLQSAKEQ IKWSLLR
