ID   GOGA4_HUMAN             Reviewed;        2230 AA.
AC   Q13439; F8W8Q7; Q13270; Q13654; Q14436; Q59EW8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   20-JAN-2016, entry version 153.
DE   RecName: Full=Golgin subfamily A member 4;
DE   AltName: Full=256 kDa golgin;
DE   AltName: Full=Golgin-245;
DE   AltName: Full=Protein 72.1;
DE   AltName: Full=Trans-Golgi p230;
GN   Name=GOLGA4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RX   PubMed=8626529; DOI=10.1074/jbc.271.14.8328;
RA   Erlich R., Gleeson P.A., Campbell P., Dietzsch E., Toh B.-H.;
RT   "Molecular characterization of trans-Golgi p230: a human peripheral
RT   membrane protein encoded by a gene on chromosome 6p12-22 contains
RT   extensive coiled-coil alpha-helical domains and a granin motif.";
RL   J. Biol. Chem. 271:8328-8337(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Seelig H.P.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1279 (ISOFORM 5).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 131-2230.
RC   TISSUE=Placenta;
RX   PubMed=8537393; DOI=10.1074/jbc.270.52.31262;
RA   Fritzler M.J., Lung C.-C., Hamel J.C., Griffith K.J., Chan E.K.L.;
RT   "Molecular characterization of golgin-245, a novel Golgi complex
RT   protein containing a granin signature.";
RL   J. Biol. Chem. 270:31262-31268(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 524-672.
RC   TISSUE=Gastric fundus;
RA   Balague C.;
RL   Thesis (1994), Instituto municipal de investigacion medica, Spain.
RN   [7]
RP   INTERACTION WITH ARL1 AND ARL3, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF TYR-2177.
RX   PubMed=11303027; DOI=10.1074/jbc.M102359200;
RA   Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT   "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
RT   specific and shared effectors: characterizing ARL1-binding proteins.";
RL   J. Biol. Chem. 276:22826-22837(2001).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MACF1.
RX   PubMed=15265687; DOI=10.1016/j.yexcr.2004.04.047;
RA   Kakinuma T., Ichikawa H., Tsukada Y., Nakamura T., Toh B.H.;
RT   "Interaction between p230 and MACF1 is associated with transport of a
RT   glycosyl phosphatidyl inositol-anchored protein from the Golgi to the
RT   cell periphery.";
RL   Exp. Cell Res. 298:388-398(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89; SER-266 AND
RP   THR-2223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-78 AND SER-266,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
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.,
RA   Buerckstuemmer T., 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-266, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
RP   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2170-2221 IN COMPLEX WITH
RP   ARL1.
RX   PubMed=14580338; DOI=10.1016/S1097-2765(03)00356-3;
RA   Panic B., Perisic O., Veprintsev D.B., Williams R.L., Munro S.;
RT   "Structural basis for Arl1-dependent targeting of homodimeric GRIP
RT   domains to the Golgi apparatus.";
RL   Mol. Cell 12:863-874(2003).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2172-2222 IN COMPLEX WITH
RP   ARL1, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-2177; VAL-2181;
RP   PHE-2183; MET-2186; THR-2193; MET-2194; VAL-2197; ILE-2198; LEU-2202;
RP   PHE-2204 AND ILE-2212, AND SUBUNIT.
RX   PubMed=14718928; DOI=10.1038/nsmb714;
RA   Wu M., Lu L., Hong W., Song H.;
RT   "Structural basis for recruitment of GRIP domain golgin-245 by small
RT   GTPase Arl1.";
RL   Nat. Struct. Mol. Biol. 11:86-94(2004).
CC   -!- FUNCTION: May play a role in delivery of transport vesicles
CC       containing GPI-linked proteins from the trans-Golgi network
CC       through its interaction with MACF1. {ECO:0000269|PubMed:15265687}.
CC   -!- SUBUNIT: Homodimer. Interacts with GTP bound ARL1. Interacts with
CC       MACF1. {ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:14580338,
CC       ECO:0000269|PubMed:14718928, ECO:0000269|PubMed:15265687}.
CC   -!- INTERACTION:
CC       Q96NW4:ANKRD27; NbExp=2; IntAct=EBI-1037845, EBI-6125599;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
CC       Peripheral membrane protein. Golgi apparatus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q13439-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q13439-3; Sequence=VSP_004274;
CC       Name=4;
CC         IsoId=Q13439-4; Sequence=VSP_004275;
CC       Name=5;
CC         IsoId=Q13439-5; Sequence=VSP_044819, VSP_004274, VSP_004275;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC   -!- MISCELLANEOUS: Antibodies against GOLGA4 are present in sera from
CC       patients with Sjoegren syndrome. Sera from patients with Sjoegren
CC       syndrome often contain antibodies that react with normal
CC       components of the Golgi complex.
CC   -!- SIMILARITY: Contains 1 GRIP domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92930.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=CAA58041.1; Type=Frameshift; Positions=2153; Evidence={ECO:0000305};
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DR   EMBL; U41740; AAC50434.1; -; mRNA.
DR   EMBL; X82834; CAA58041.1; ALT_FRAME; mRNA.
DR   EMBL; AC097359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB209693; BAD92930.1; ALT_INIT; mRNA.
DR   EMBL; U31906; AAC51791.1; -; mRNA.
DR   EMBL; X76942; CAA54261.1; -; mRNA.
DR   CCDS; CCDS2666.1; -. [Q13439-1]
DR   CCDS; CCDS54564.1; -. [Q13439-5]
DR   RefSeq; NP_001166184.1; NM_001172713.1. [Q13439-5]
DR   RefSeq; NP_002069.2; NM_002078.4. [Q13439-1]
DR   UniGene; Hs.344151; -.
DR   PDB; 1R4A; X-ray; 2.30 A; E/F/G/H=2172-2222.
DR   PDB; 1UPT; X-ray; 1.70 A; B/D/F/H=2170-2228.
DR   PDBsum; 1R4A; -.
DR   PDBsum; 1UPT; -.
DR   ProteinModelPortal; Q13439; -.
DR   SMR; Q13439; 2172-2222.
DR   BioGrid; 109065; 19.
DR   IntAct; Q13439; 20.
DR   MINT; MINT-3027757; -.
DR   STRING; 9606.ENSP00000349305; -.
DR   iPTMnet; Q13439; -.
DR   PhosphoSite; Q13439; -.
DR   UniCarbKB; Q13439; -.
DR   BioMuta; GOLGA4; -.
DR   DMDM; 12643718; -.
DR   MaxQB; Q13439; -.
DR   PaxDb; Q13439; -.
DR   PRIDE; Q13439; -.
DR   Ensembl; ENST00000356847; ENSP00000349305; ENSG00000144674. [Q13439-5]
DR   Ensembl; ENST00000361924; ENSP00000354486; ENSG00000144674. [Q13439-1]
DR   GeneID; 2803; -.
DR   KEGG; hsa:2803; -.
DR   UCSC; uc003cgv.3; human. [Q13439-1]
DR   UCSC; uc003cgx.3; human. [Q13439-4]
DR   CTD; 2803; -.
DR   GeneCards; GOLGA4; -.
DR   HGNC; HGNC:4427; GOLGA4.
DR   HPA; HPA035102; -.
DR   HPA; HPA040675; -.
DR   MIM; 602509; gene.
DR   neXtProt; NX_Q13439; -.
DR   PharmGKB; PA28808; -.
DR   eggNOG; ENOG410IEA5; Eukaryota.
DR   eggNOG; ENOG410XQQG; LUCA.
DR   GeneTree; ENSGT00730000111139; -.
DR   HOGENOM; HOG000112753; -.
DR   HOVERGEN; HBG051754; -.
DR   InParanoid; Q13439; -.
DR   OMA; STKFSEW; -.
DR   OrthoDB; EOG72C4ZF; -.
DR   PhylomeDB; Q13439; -.
DR   TreeFam; TF325082; -.
DR   ChiTaRS; GOLGA4; human.
DR   EvolutionaryTrace; Q13439; -.
DR   GeneWiki; GOLGA4; -.
DR   GenomeRNAi; 2803; -.
DR   NextBio; 11049; -.
DR   PRO; PR:Q13439; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; Q13439; -.
DR   CleanEx; HS_GOLGA4; -.
DR   ExpressionAtlas; Q13439; baseline and differential.
DR   Genevisible; Q13439; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:ProtInc.
DR   GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR   GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
DR   GO; GO:0000042; P:protein targeting to Golgi; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR   Gene3D; 1.10.220.60; -; 1.
DR   InterPro; IPR000237; GRIP.
DR   Pfam; PF01465; GRIP; 1.
DR   SMART; SM00755; Grip; 1.
DR   SUPFAM; SSF101283; SSF101283; 1.
DR   PROSITE; PS50913; GRIP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW   Cytoplasm; Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein;
KW   Polymorphism; Reference proteome.
FT   CHAIN         1   2230       Golgin subfamily A member 4.
FT                                /FTId=PRO_0000190059.
FT   DOMAIN     2168   2215       GRIP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00250}.
FT   REGION      133    203       Interaction with MACF1.
FT   COILED      133   2185       {ECO:0000255}.
FT   COMPBIAS    252   2096       Glu-rich.
FT   MOD_RES      39     39       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q91VW5}.
FT   MOD_RES      71     71       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      78     78       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES      89     89       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     266    266       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES    2223   2223       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   CARBOHYD    585    585       N-linked (GlcNAc...).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1612   1612       N-linked (GlcNAc...).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   VAR_SEQ      54     54       E -> ENASTHASKSPDSVNGSEPSIPQ (in isoform
FT                                5). {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_044819.
FT   VAR_SEQ    2103   2109       Missing (in isoform 3 and isoform 5).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_004274.
FT   VAR_SEQ    2222   2230       FTSPRSGIF -> SWLRSSS (in isoform 4 and
FT                                isoform 5). {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_004275.
FT   VARIANT    1028   1028       Q -> K (in dbSNP:rs11718848).
FT                                /FTId=VAR_033975.
FT   VARIANT    1552   1552       N -> S (in dbSNP:rs9840779).
FT                                /FTId=VAR_033976.
FT   VARIANT    2058   2058       R -> S (in dbSNP:rs11924014).
FT                                /FTId=VAR_049258.
FT   MUTAGEN    2177   2177       Y->A: Loss of Golgi membrane
FT                                localization. Loss of ARL1-binding.
FT                                {ECO:0000269|PubMed:11303027,
FT                                ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2177   2177       Y->F: No effect.
FT                                {ECO:0000269|PubMed:11303027,
FT                                ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2181   2181       V->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2183   2183       F->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2186   2186       M->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2193   2193       T->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2194   2194       M->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2197   2197       V->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2198   2198       I->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2202   2202       L->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2204   2204       F->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   MUTAGEN    2212   2212       I->A: Abolishes Golgi localization.
FT                                {ECO:0000269|PubMed:14718928}.
FT   CONFLICT    188    188       R -> K (in Ref. 5; AAC51791).
FT                                {ECO:0000305}.
FT   CONFLICT    220    220       Y -> H (in Ref. 5; AAC51791).
FT                                {ECO:0000305}.
FT   CONFLICT    276    276       T -> A (in Ref. 5; AAC51791).
FT                                {ECO:0000305}.
FT   CONFLICT    584    584       K -> E (in Ref. 5; AAC51791).
FT                                {ECO:0000305}.
FT   CONFLICT    628    628       T -> A (in Ref. 5; AAC51791).
FT                                {ECO:0000305}.
FT   CONFLICT    630    630       K -> E (in Ref. 5; AAC51791).
FT                                {ECO:0000305}.
FT   CONFLICT    682    682       K -> N (in Ref. 5; AAC51791).
FT                                {ECO:0000305}.
FT   HELIX      2173   2186       {ECO:0000244|PDB:1UPT}.
FT   HELIX      2191   2201       {ECO:0000244|PDB:1UPT}.
FT   HELIX      2206   2225       {ECO:0000244|PDB:1UPT}.
SQ   SEQUENCE   2230 AA;  261140 MW;  3BB733DB1EA86134 CRC64;
     MFKKLKQKIS EEQQQLQQAL APAQASSNSS TPTRMRSRTS SFTEQLDEGT PNRESGDTQS
     FAQKLQLRVP SVESLFRSPI KESLFRSSSK ESLVRTSSRE SLNRLDLDSS TASFDPPSDM
     DSEAEDLVGN SDSLNKEQLI QRLRRMERSL SSYRGKYSEL VTAYQMLQRE KKKLQGILSQ
     SQDKSLRRIA ELREELQMDQ QAKKHLQEEF DASLEEKDQY ISVLQTQVSL LKQRLRNGPM
     NVDVLKPLPQ LEPQAEVFTK EENPESDGEP VVEDGTSVKT LETLQQRVKR QENLLKRCKE
     TIQSHKEQCT LLTSEKEALQ EQLDERLQEL EKIKDLHMAE KTKLITQLRD AKNLIEQLEQ
     DKGMVIAETK RQMHETLEMK EEEIAQLRSR IKQMTTQGEE LREQKEKSER AAFEELEKAL
     STAQKTEEAR RKLKAEMDEQ IKTIEKTSEE ERISLQQELS RVKQEVVDVM KKSSEEQIAK
     LQKLHEKELA RKEQELTKKL QTREREFQEQ MKVALEKSQS EYLKISQEKE QQESLALEEL
     ELQKKAILTE SENKLRDLQQ EAETYRTRIL ELESSLEKSL QENKNQSKDL AVHLEAEKNK
     HNKEITVMVE KHKTELESLK HQQDALWTEK LQVLKQQYQT EMEKLREKCE QEKETLLKDK
     EIIFQAHIEE MNEKTLEKLD VKQTELESLS SELSEVLKAR HKLEEELSVL KDQTDKMKQE
     LEAKMDEQKN HHQQQVDSII KEHEVSIQRT EKALKDQINQ LELLLKERDK HLKEHQAHVE
     NLEADIKRSE GELQQASAKL DVFQSYQSAT HEQTKAYEEQ LAQLQQKLLD LETERILLTK
     QVAEVEAQKK DVCTELDAHK IQVQDLMQQL EKQNSEMEQK VKSLTQVYES KLEDGNKEQE
     QTKQILVEKE NMILQMREGQ KKEIEILTQK LSAKEDSIHI LNEEYETKFK NQEKKMEKVK
     QKAKEMQETL KKKLLDQEAK LKKELENTAL ELSQKEKQFN AKMLEMAQAN SAGISDAVSR
     LETNQKEQIE SLTEVHRREL NDVISIWEKK LNQQAEELQE IHEIQLQEKE QEVAELKQKI
     LLFGCEKEEM NKEITWLKEE GVKQDTTLNE LQEQLKQKSA HVNSLAQDET KLKAHLEKLE
     VDLNKSLKEN TFLQEQLVEL KMLAEEDKRK VSELTSKLKT TDEEFQSLKS SHEKSNKSLE
     DKSLEFKKLS EELAIQLDIC CKKTEALLEA KTNELINISS SKTNAILSRI SHCQHRTTKV
     KEALLIKTCT VSELEAQLRQ LTEEQNTLNI SFQQATHQLE EKENQIKSMK ADIESLVTEK
     EALQKEGGNQ QQAASEKESC ITQLKKELSE NINAVTLMKE ELKEKKVEIS SLSKQLTDLN
     VQLQNSISLS EKEAAISSLR KQYDEEKCEL LDQVQDLSFK VDTLSKEKIS ALEQVDDWSN
     KFSEWKKKAQ SRFTQHQNTV KELQIQLELK SKEAYEKDEQ INLLKEELDQ QNKRFDCLKG
     EMEDDKSKME KKESNLETEL KSQTARIMEL EDHITQKTIE IESLNEVLKN YNQQKDIEHK
     ELVQKLQHFQ ELGEEKDNRV KEAEEKILTL ENQVYSMKAE LETKKKELEH VNLSVKSKEE
     ELKALEDRLE SESAAKLAEL KRKAEQKIAA IKKQLLSQME EKEEQYKKGT ESHLSELNTK
     LQEREREVHI LEEKLKSVES SQSETLIVPR SAKNVAAYTE QEEADSQGCV QKTYEEKISV
     LQRNLTEKEK LLQRVGQEKE ETVSSHFEMR CQYQERLIKL EHAEAKQHED QSMIGHLQEE
     LEEKNKKYSL IVAQHVEKEG GKNNIQAKQN LENVFDDVQK TLQEKELTCQ ILEQKIKELD
     SCLVRQKEVH RVEMEELTSK YEKLQALQQM DGRNKPTELL EENTEEKSKS HLVQPKLLSN
     MEAQHNDLEF KLAGAEREKQ KLGKEIVRLQ KDLRMLRKEH QQELEILKKE YDQEREEKIK
     QEQEDLELKH NSTLKQLMRE FNTQLAQKEQ ELEMTIKETI NKAQEVEAEL LESHQEETNQ
     LLKKIAEKDD DLKRTAKRYE EILDAREEEM TAKVRDLQTQ LEELQKKYQQ KLEQEENPGN
     DNVTIMELQT QLAQKTTLIS DSKLKEQEFR EQIHNLEDRL KKYEKNVYAT TVGTPYKGGN
     LYHTDVSLFG EPTEFEYLRK VLFEYMMGRE TKTMAKVITT VLKFPDDQTQ KILEREDARL
     MFTSPRSGIF
//