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 27-MAR-2024, entry version 209. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 extensive RT 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., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., 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., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., 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 protein RT 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 RAB6A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-2177. RX PubMed=10209123; DOI=10.1016/s0960-9822(99)80167-5; RA Barr F.A.; RT "A novel Rab6-interacting domain defines a family of Golgi-targeted coiled- RT coil proteins."; RL Curr. Biol. 9:381-384(1999). RN [8] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-2177 AND TYR-2185. RX PubMed=10209125; DOI=10.1016/s0960-9822(99)80168-7; RA Kjer-Nielsen L., Teasdale R.D., van Vliet C., Gleeson P.A.; RT "A novel Golgi-localisation domain shared by a class of coiled-coil RT peripheral membrane proteins."; RL Curr. Biol. 9:385-388(1999). RN [9] RP INTERACTION WITH ARL1 AND ARL3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 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 specific RT and shared effectors: characterizing ARL1-binding proteins."; RL J. Biol. Chem. 276:22826-22837(2001). RN [10] 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 cell RT periphery."; RL Exp. Cell Res. 298:388-398(2004). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89; SER-266 AND RP THR-2223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12] 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., 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY RP 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-78 AND SER-266, AND RP 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] 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 [16] 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., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-41; SER-71; SER-78 RP AND SER-266, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, 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 [19] RP FUNCTION, INTERACTION WITH TBC1D23 AND FAM91A1, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF PHE-2. RX PubMed=29084197; DOI=10.1038/ncb3627; RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.; RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at RT the trans-Golgi."; RL Nat. Cell Biol. 19:1424-1432(2017). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2170-2221 IN COMPLEX WITH 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 domains RT to the Golgi apparatus."; RL Mol. Cell 12:863-874(2003). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2172-2222 IN COMPLEX WITH ARL1, RP SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-2181; PHE-2183; MET-2186; RP THR-2193; MET-2194; VAL-2197; ILE-2198; LEU-2202; PHE-2204 AND ILE-2212, RP AND HOMODIMERIZATION. 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 GTPase RT Arl1."; RL Nat. Struct. Mol. Biol. 11:86-94(2004). CC -!- FUNCTION: Involved in vesicular trafficking at the Golgi apparatus CC level. May play a role in delivery of transport vesicles containing CC GPI-linked proteins from the trans-Golgi network through its CC interaction with MACF1. Involved in endosome-to-Golgi trafficking CC (PubMed:29084197). {ECO:0000269|PubMed:15265687, CC ECO:0000269|PubMed:29084197}. CC -!- SUBUNIT: Homodimer (PubMed:14718928). Interacts with RAB6A CC (PubMed:10209123). Interacts with GTP-bound ARL1 and ARL3 CC (PubMed:11303027, PubMed:14580338, PubMed:14718928). Interacts with CC MACF1 (PubMed:15265687). Directly interacts with TBC1D23 CC (PubMed:29084197). Interacts with FAM91A1; this interaction may be CC mediated by TBC1D23 (PubMed:29084197). {ECO:0000269|PubMed:10209123, CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:14580338, CC ECO:0000269|PubMed:14718928, ECO:0000269|PubMed:15265687, CC ECO:0000269|PubMed:29084197}. CC -!- INTERACTION: CC Q13439; Q96NW4: ANKRD27; NbExp=2; IntAct=EBI-1037845, EBI-6125599; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane CC {ECO:0000269|PubMed:10209123, ECO:0000269|PubMed:10209125, CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:14718928, CC ECO:0000269|PubMed:15265687}; Peripheral membrane protein. Golgi CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:29084197}. 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 -!- 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 components of CC the Golgi complex. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92930.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA58041.1; Type=Frameshift; Evidence={ECO:0000305}; 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; 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 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 AlphaFoldDB; Q13439; -. DR SMR; Q13439; -. DR BioGRID; 109065; 227. DR IntAct; Q13439; 54. DR MINT; Q13439; -. DR STRING; 9606.ENSP00000349305; -. DR GlyConnect; 690; 5 N-Linked glycans (2 sites). DR GlyCosmos; Q13439; 2 sites, 10 glycans. DR GlyGen; Q13439; 3 sites, 10 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q13439; -. DR MetOSite; Q13439; -. DR PhosphoSitePlus; Q13439; -. DR BioMuta; GOLGA4; -. DR DMDM; 12643718; -. DR EPD; Q13439; -. DR jPOST; Q13439; -. DR MassIVE; Q13439; -. DR MaxQB; Q13439; -. DR PaxDb; 9606-ENSP00000349305; -. DR PeptideAtlas; Q13439; -. DR ProteomicsDB; 30188; -. DR ProteomicsDB; 59436; -. [Q13439-1] DR ProteomicsDB; 59437; -. [Q13439-3] DR ProteomicsDB; 59438; -. [Q13439-4] DR Pumba; Q13439; -. DR Antibodypedia; 28305; 115 antibodies from 23 providers. DR DNASU; 2803; -. DR Ensembl; ENST00000356847.8; ENSP00000349305.4; ENSG00000144674.19. [Q13439-5] DR Ensembl; ENST00000361924.7; ENSP00000354486.2; ENSG00000144674.19. [Q13439-1] DR GeneID; 2803; -. DR KEGG; hsa:2803; -. DR MANE-Select; ENST00000361924.7; ENSP00000354486.2; NM_002078.5; NP_002069.2. DR UCSC; uc003cgv.4; human. [Q13439-1] DR AGR; HGNC:4427; -. DR CTD; 2803; -. DR DisGeNET; 2803; -. DR GeneCards; GOLGA4; -. DR HGNC; HGNC:4427; GOLGA4. DR HPA; ENSG00000144674; Low tissue specificity. DR MIM; 602509; gene. DR neXtProt; NX_Q13439; -. DR OpenTargets; ENSG00000144674; -. DR PharmGKB; PA28808; -. DR VEuPathDB; HostDB:ENSG00000144674; -. DR eggNOG; ENOG502QTM0; Eukaryota. DR GeneTree; ENSGT00730000111139; -. DR HOGENOM; CLU_001994_0_0_1; -. DR InParanoid; Q13439; -. DR OMA; KAIIHVD; -. DR OrthoDB; 5400687at2759; -. DR PhylomeDB; Q13439; -. DR TreeFam; TF325082; -. DR PathwayCommons; Q13439; -. DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network. DR Reactome; R-HSA-9673768; Signaling by membrane-tethered fusions of PDGFRA or PDGFRB. DR SignaLink; Q13439; -. DR BioGRID-ORCS; 2803; 14 hits in 1154 CRISPR screens. DR ChiTaRS; GOLGA4; human. DR EvolutionaryTrace; Q13439; -. DR GeneWiki; GOLGA4; -. DR GenomeRNAi; 2803; -. DR Pharos; Q13439; Tbio. DR PRO; PR:Q13439; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q13439; Protein. DR Bgee; ENSG00000144674; Expressed in gluteal muscle and 212 other cell types or tissues. DR ExpressionAtlas; Q13439; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005802; C:trans-Golgi network; TAS:ProtInc. DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB. DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central. DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc. DR Gene3D; 1.10.287.1490; -; 1. DR Gene3D; 1.10.220.60; GRIP domain; 1. DR InterPro; IPR000237; GRIP_dom. DR PANTHER; PTHR19327; GOLGIN; 1. DR PANTHER; PTHR19327:SF0; GOLGIN SUBFAMILY A MEMBER 4; 1. DR Pfam; PF01465; GRIP; 1. DR SMART; SM00755; Grip; 1. DR SUPFAM; SSF101283; GRIP domain; 1. DR PROSITE; PS50913; GRIP; 1. DR Genevisible; Q13439; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Glycoprotein; KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome. FT CHAIN 1..2230 FT /note="Golgin subfamily A member 4" FT /id="PRO_0000190059" FT DOMAIN 2168..2215 FT /note="GRIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250" FT REGION 1..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 87..127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 133..203 FT /note="Interaction with MACF1" FT /evidence="ECO:0000269|PubMed:15265687" FT COILED 133..2185 FT /evidence="ECO:0000255" FT COMPBIAS 11..64 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..117 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 39 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q91VW5" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 78 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2223 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CARBOHYD 585 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1612 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT VAR_SEQ 54 FT /note="E -> ENASTHASKSPDSVNGSEPSIPQ (in isoform 5)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_044819" FT VAR_SEQ 2103..2109 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_004274" FT VAR_SEQ 2222..2230 FT /note="FTSPRSGIF -> SWLRSSS (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_004275" FT VARIANT 1028 FT /note="Q -> K (in dbSNP:rs11718848)" FT /id="VAR_033975" FT VARIANT 1552 FT /note="N -> S (in dbSNP:rs9840779)" FT /id="VAR_033976" FT VARIANT 2058 FT /note="R -> S (in dbSNP:rs11924014)" FT /id="VAR_049258" FT MUTAGEN 2 FT /note="F->A: Loss of TBC1D23-binding." FT /evidence="ECO:0000269|PubMed:29084197" FT MUTAGEN 2177 FT /note="Y->A: Loss of localization at the Golgi apparatus. FT Loss of ARL1-binding." FT /evidence="ECO:0000269|PubMed:10209123, FT ECO:0000269|PubMed:10209125, ECO:0000269|PubMed:11303027, FT ECO:0000269|PubMed:14718928" FT MUTAGEN 2177 FT /note="Y->F: No effect on localization at the Golgi FT apparatus." FT /evidence="ECO:0000269|PubMed:10209125, FT ECO:0000269|PubMed:14718928" FT MUTAGEN 2181 FT /note="V->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2183 FT /note="F->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2185 FT /note="Y->A: Loss of localization at the Golgi apparatus." FT /evidence="ECO:0000269|PubMed:10209125" FT MUTAGEN 2186 FT /note="M->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2193 FT /note="T->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2194 FT /note="M->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2197 FT /note="V->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2198 FT /note="I->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2202 FT /note="L->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2204 FT /note="F->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT MUTAGEN 2212 FT /note="I->A: Abolishes Golgi localization." FT /evidence="ECO:0000269|PubMed:14718928" FT CONFLICT 188 FT /note="R -> K (in Ref. 5; AAC51791)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="Y -> H (in Ref. 5; AAC51791)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="T -> A (in Ref. 5; AAC51791)" FT /evidence="ECO:0000305" FT CONFLICT 584 FT /note="K -> E (in Ref. 5; AAC51791)" FT /evidence="ECO:0000305" FT CONFLICT 628 FT /note="T -> A (in Ref. 5; AAC51791)" FT /evidence="ECO:0000305" FT CONFLICT 630 FT /note="K -> E (in Ref. 5; AAC51791)" FT /evidence="ECO:0000305" FT CONFLICT 682 FT /note="K -> N (in Ref. 5; AAC51791)" FT /evidence="ECO:0000305" FT HELIX 2173..2186 FT /evidence="ECO:0007829|PDB:1UPT" FT HELIX 2191..2201 FT /evidence="ECO:0007829|PDB:1UPT" FT HELIX 2206..2221 FT /evidence="ECO:0007829|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 //