ID GCP60_HUMAN Reviewed; 528 AA. AC Q9H3P7; B2RB29; Q5VTJ0; Q6P9F1; Q8IZC5; Q8N4D6; Q9H6U3; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 179. DE RecName: Full=Golgi resident protein GCP60; DE AltName: Full=Acyl-CoA-binding domain-containing protein 3; DE AltName: Full=Golgi complex-associated protein 1; DE Short=GOCAP1; DE AltName: Full=Golgi phosphoprotein 1; DE Short=GOLPH1; DE AltName: Full=PBR- and PKA-associated protein 7; DE AltName: Full=Peripheral benzodiazepine receptor-associated protein PAP7; DE Contains: DE RecName: Full=Golgi resident protein GCP60, N-terminally processed; GN Name=ACBD3; Synonyms=GCP60, GOCAP1, GOLPH1; 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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION RP WITH GOLGB1, AND TISSUE SPECIFICITY. RC TISSUE=Cervix carcinoma; RX PubMed=11590181; DOI=10.1074/jbc.m108961200; RA Sohda M., Misumi Y., Yamamoto A., Yano A., Nakamura N., Ikehara Y.; RT "Identification and characterization of a novel Golgi protein, GCP60, that RT interacts with the integral membrane protein giantin."; RL J. Biol. Chem. 276:45298-45306(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-187. RC TISSUE=Placenta; RA Liu J., Tobin D., Tasken K., Papadopoulos V.; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-187. RC TISSUE=Trachea; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Ovary; 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 [7] RP PROTEIN SEQUENCE OF 1-188; 231-406 AND 467-528, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION, INTERACTION WITH PI4KB, RP INTERACTION WITH TBC1D22A, INTERACTION WITH TBC1D22B, MUTAGENESIS OF RP LYS-243; GLN-244; GLN-245; ILE-246; GLN-253; THR-254; 256-VAL--PHE-258; RP GLN-257; PHE-258; GLN-259; GLN-260; TYR-261; 264-GLN--TYR-266; RP 267-PRO--ASN-269; ILE-275; LEU-276; 282-GLU--TYR-285; HIS-284; TYR-285; RP GLN-286; GLN-287; TYR-288; 344-SER-SER-345; 414-SER--LEU-416; RP 417-PHE--PHE-420; 433-PHE--TRP-435; 494-GLY--HIS-496; SER-511 AND RP 511-SER--SER-513, MASS SPECTROMETRY, INTERACTION WITH HEPATITIS A VIRUS RP PROTEIN 3A (MICROBIAL INFECTION), INTERACTION WITH HUMAN PARECHOVIRUS 1 RP PROTEIN 3A (MICROBIAL INFECTION), INTERACTION WITH HUMAN KLASSEVIRUS RP PROTEIN 3A (MICROBIAL INFECTION), INTERACTION WITH AICHI VIRUS PROTEIN 3A, RP INTERACTION WITH POLIOVIRUS PROTEIN 3A, DOMAIN, AND SUBUNIT. RX PubMed=23572552; DOI=10.1128/mbio.00098-13; RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.; RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected RT by enteroviral and kobuviral 3A protein binding."; RL MBio 4:E00098-E00098(2013). RN [8] RP PROTEIN SEQUENCE OF 2-9, AND CLEAVAGE OF INITIATOR METHIONINE. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, 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=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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-20, 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 [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 FUNCTION (MICROBIAL INFECTION), INTERACTION WITH AICHI VIRUS PROTEIN 3A RP (MICROBIAL INFECTION), INTERACTION WITH AICHI VIRUS PROTEIN 2B (MICROBIAL RP INFECTION), INTERACTION WITH AICHI VIRUS PROTEIN 2C (MICROBIAL INFECTION), RP INTERACTION WITH PI4KB, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A RP COMPLEX AICHI VIRUS PROTEIN 3A/ACBD3/PI4KB (MICROBIAL INFECTION). RX PubMed=22124328; DOI=10.1038/emboj.2011.429; RA Sasaki J., Ishikawa K., Arita M., Taniguchi K.; RT "ACBD3-mediated recruitment of PI4KB to picornavirus RNA replication RT sites."; RL EMBO J. 31:754-766(2012). RN [14] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH AICHI VIRUS PROTEIN 3A RP (MICROBIAL INFECTION), INTERACTION WITH POLIOVIRUS VIRUS PROTEIN 3A RP (MICROBIAL INFECTION), INTERACTION WITH HRV14 PROTEIN 3A (MICROBIAL RP INFECTION), INTERACTION WITH COXSACKIEVIRUS B2 PROTEIN 3A (MICROBIAL RP INFECTION), INTERACTION WITH COXSACKIEVIRUS B3 PROTEIN 3A (MICROBIAL RP INFECTION), INTERACTION WITH COXSACKIEVIRUS B5 PROTEIN 3A (MICROBIAL RP INFECTION), INTERACTION WITH PI4KB, AND IDENTIFICATION IN A COMPLEX AICHI RP VIRUS PROTEIN 3A/ACBD3/PI4KB (MICROBIAL INFECTION). RX PubMed=22258260; DOI=10.1128/jvi.06778-11; RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., Derisi J.L.; RT "The 3A protein from multiple picornaviruses utilizes the golgi adaptor RT protein ACBD3 to recruit PI4KIIIbeta."; RL J. Virol. 86:3605-3616(2012). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 THR-18; SER-43 AND SER-47, AND 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 [19] RP IDENTIFICATION IN A COMPLEX AICHI VIRUS PROTEIN 3A/ACBD3/PI4KB (MICROBIAL RP INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=30755512; DOI=10.1128/mbio.02742-18; RA Lyoo H., van der Schaar H.M., Dorobantu C.M., Rabouw H.H., RA Strating J.R.P.M., van Kuppeveld F.J.M.; RT "ACBD3 is an essential pan-enterovirus host factor that mediates the RT interaction between viral 3A protein and cellular protein PI4KB."; RL MBio 10:0-0(2019). RN [20] {ECO:0007744|PDB:2N72, ECO:0007744|PDB:2N73} RP STRUCTURE BY NMR OF 241-308 IN COMPLEX WITH PI4KB, FUNCTION, INTERACTION RP WITH PI4KB, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-258; TYR-266; RP HIS-284; TYR-285 AND TYR-288. RX PubMed=27009356; DOI=10.1038/srep23641; RA Klima M., Toth D.J., Hexnerova R., Baumlova A., Chalupska D., Tykvart J., RA Rezabkova L., Sengupta N., Man P., Dubankova A., Humpolickova J., RA Nencka R., Veverka V., Balla T., Boura E.; RT "Structural insights and in vitro reconstitution of membrane targeting and RT activation of human PI4KB by the ACBD3 protein."; RL Sci. Rep. 6:23641-23641(2016). RN [21] {ECO:0007744|PDB:5TDQ} RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 367-528, FUNCTION (MICROBIAL RP INFECTION), INTERACTION WITH PI4KB, INTERACTION WITH AICHI VIRUS 3A PROTEIN RP (MICROBIAL INFECTION), MUTAGENESIS OF 258-PHE-GLN-259; 380-ILE-LYS-381 AND RP TYR-525, IDENTIFICATION IN A COMPLEX AICHI VIRUS PROTEIN 3A/ACBD3/PI4KB RP (MICROBIAL INFECTION), AND DOMAIN (MICROBIAL INFECTION). RX PubMed=27989622; DOI=10.1016/j.str.2016.11.016; RA McPhail J.A., Ottosen E.H., Jenkins M.L., Burke J.E.; RT "The molecular basis of Aichi virus 3A protein activation of RT phosphatidylinositol 4 kinase IIIbeta, PI4KB, through ACBD3."; RL Structure 25:121-131(2017). RN [22] {ECO:0007744|PDB:5LZ1, ECO:0007744|PDB:5LZ3, ECO:0007744|PDB:5LZ6} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 364-528, AND INTERACTION WITH RP AICHI VIRUS PROTEIN 3A (MICROBIAL INFECTION). RX PubMed=28065508; DOI=10.1016/j.str.2016.11.021; RA Klima M., Chalupska D., Rozycki B., Humpolickova J., Rezabkova L., RA Silhan J., Baumlova A., Dubankova A., Boura E.; RT "Kobuviral Non-structural 3A Proteins Act as Molecular Harnesses to Hijack RT the Host ACBD3 Protein."; RL Structure 25:219-230(2017). RN [23] {ECO:0007744|PDB:6HLN, ECO:0007744|PDB:6HLT, ECO:0007744|PDB:6HLV, ECO:0007744|PDB:6HLW, ECO:0007744|PDB:6HM8, ECO:0007744|PDB:6HMV} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 364-528, MUTAGENESIS OF RP 514-LEU--ARG-516, SUBCELLULAR LOCATION, INTERACTION WITH POLIOVIRUS PROTEIN RP 3A, INTERACTION WITH ENTEROVIRUS A71 PROTEIN 3A, INTERACTION WITH RP ENTEROVIRUS D68 PROTEIN 3A, INTERACTION WITH RHINOVIRUS B14 PROTEIN 3A, RP INTERACTION WITH COXSACKIEVIRUS B3 PROTEIN 3A, AND MUTAGENESIS OF RP 375-TRP--ARG-377; 403-VAL--VAL-407; 414-SER--PHE-417 AND 523-ARG--THR-527. RX PubMed=31381608; DOI=10.1371/journal.ppat.1007962; RA Horova V., Lyoo H., Rozycki B., Chalupska D., Smola M., Humpolickova J., RA Strating J.R.P.M., van Kuppeveld F.J.M., Boura E., Klima M.; RT "Convergent evolution in the mechanisms of ACBD3 recruitment to RT picornavirus replication sites."; RL PLoS Pathog. 15:E1007962-E1007962(2019). CC -!- FUNCTION: Involved in the maintenance of Golgi structure by interacting CC with giantin, affecting protein transport between the endoplasmic CC reticulum and Golgi (PubMed:11590181). Involved in hormone-induced CC steroid biosynthesis in testicular Leydig cells (By similarity). CC Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme CC activity of PI4KB activity via its membrane recruitment thereby CC increasing the local concentration of the substrate in the vicinity of CC the kinase (PubMed:27009356). {ECO:0000250|UniProtKB:Q8BMP6, CC ECO:0000269|PubMed:11590181, ECO:0000269|PubMed:27009356}. CC -!- FUNCTION: (Microbial infection) Plays an essential role in Aichi virus CC RNA replication by recruiting PI4KB at the viral replication sites. CC {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:22258260, CC ECO:0000269|PubMed:27989622}. CC -!- SUBUNIT: Homodimer (PubMed:23572552). Interacts with the C-terminal CC cytoplasmic domain of giantin/GOLGB1 (PubMed:11590181). Interacts with CC PBR and PKA regulatory subunit RI-alpha. Does not interact with PKA CC regulatory subunit RI-beta nor PKA regulatory subunit RII-alpha (By CC similarity). Interacts (via Q domain) with PI4KB (via N-terminus) CC (PubMed:23572552, PubMed:27009356, PubMed:27989622, PubMed:22124328, CC PubMed:22258260). Interacts (via Q domain) with TBC1D22A and TBC1D22B; CC interactions with PI4KB and with TBC1D22A and TBC1D22B are mutually CC exclusive (PubMed:23572552, PubMed:27009356, PubMed:27989622, CC PubMed:22124328). Interacts with C10ORF76 and RAB11B (PubMed:23572552). CC {ECO:0000250|UniProtKB:Q8BMP6, ECO:0000269|PubMed:11590181, CC ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:22258260, CC ECO:0000269|PubMed:23572552, ECO:0000269|PubMed:27009356, CC ECO:0000269|PubMed:27989622}. CC -!- SUBUNIT: (Microbial infection) Interacts (via GOLD domain) with 3A CC proteins from various picornaviruses, including poliovirus, enterovirus CC A71, enterovirus D68, hepatitis A virus, human parechovirus 1, CC poliovirus, Human rhinovirus-14 (Hrv-14), coysackievirus B2, CC coysackievirus B3, coysackievirus B5, Aichi virus and human klassevirus CC (PubMed:23572552, PubMed:22258260, PubMed:31381608). Interacts (via CC GOLD domain) with Aichi virus protein 3A; this interaction allows the CC formation of a 3A/ACBD3/PI4KB complex in order to synthesize PI4P at CC the viral RNA replication sites (PubMed:23572552, PubMed:22124328, CC PubMed:27989622, PubMed:30755512) (Probable). Interacts with Aichi CC virus protein 2B (PubMed:22124328). Interacts with Aichi virus protein CC 2C (PubMed:22124328). {ECO:0000269|PubMed:22124328, CC ECO:0000269|PubMed:22258260, ECO:0000269|PubMed:23572552, CC ECO:0000269|PubMed:27989622, ECO:0000269|PubMed:30755512, CC ECO:0000269|PubMed:31381608, ECO:0000305|PubMed:28065508}. CC -!- INTERACTION: CC Q9H3P7; A0A0B4J1S8: PI4KB; NbExp=6; IntAct=EBI-1791792, EBI-21229583; CC Q9H3P7; Q9UBF8: PI4KB; NbExp=4; IntAct=EBI-1791792, EBI-1053214; CC Q9H3P7; Q8WUA7: TBC1D22A; NbExp=13; IntAct=EBI-1791792, EBI-2821276; CC Q9H3P7; Q9NU19: TBC1D22B; NbExp=6; IntAct=EBI-1791792, EBI-8787464; CC Q9H3P7; Q8BHN0: Ppm1l; Xeno; NbExp=3; IntAct=EBI-1791792, EBI-7970002; CC Q9H3P7; O91464; Xeno; NbExp=13; IntAct=EBI-1791792, EBI-7587528; CC Q9H3P7; PRO_0000448012 [O91464]; Xeno; NbExp=4; IntAct=EBI-1791792, EBI-22117245; CC Q9H3P7; PRO_0000448014 [O91464]; Xeno; NbExp=5; IntAct=EBI-1791792, EBI-22117252; CC Q9H3P7; PRO_0000448015 [O91464]; Xeno; NbExp=5; IntAct=EBI-1791792, EBI-22116975; CC Q9H3P7; PRO_0000424692 [P03300]; Xeno; NbExp=12; IntAct=EBI-1791792, EBI-21242141; CC Q9H3P7; PRO_0000039600 [Q66282]; Xeno; NbExp=2; IntAct=EBI-1791792, EBI-21242149; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:27009356, CC ECO:0000269|PubMed:30755512, ECO:0000269|PubMed:31381608}; Peripheral CC membrane protein {ECO:0000305|PubMed:31381608}; Cytoplasmic side CC {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Also mitochondrial CC (via its interaction with PBR). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in testis and CC ovary. {ECO:0000269|PubMed:11590181}. CC -!- DOMAIN: The central Gln-rich region (Q domain) is involved in binding CC to PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). The C-terminal GOLD CC domain is essential for giantin binding. The GOLD domain is also CC involved in homodimerization (PubMed:23572552). CC {ECO:0000269|PubMed:23572552}. CC -!- DOMAIN: (Microbial infection) The GOLD domain is involved in binding to CC the picornaviral protein 3A. {ECO:0000269|PubMed:23572552, CC ECO:0000269|PubMed:27989622}. 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; AB043587; BAB20592.2; -; mRNA. DR EMBL; AY150218; AAN60219.1; -; mRNA. DR EMBL; AK025520; BAB15159.1; -; mRNA. DR EMBL; AK314468; BAG37076.1; -; mRNA. DR EMBL; AL592045; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471098; EAW69775.1; -; Genomic_DNA. DR EMBL; BC034563; AAH34563.2; -; mRNA. DR EMBL; BC045533; AAH45533.1; -; mRNA. DR EMBL; BC060792; AAH60792.1; -; mRNA. DR CCDS; CCDS1551.1; -. DR RefSeq; NP_073572.2; NM_022735.3. DR PDB; 2N72; NMR; -; A=241-308. DR PDB; 2N73; NMR; -; A=241-308. DR PDB; 5LZ1; X-ray; 2.00 A; A=364-528. DR PDB; 5LZ3; X-ray; 3.00 A; A=364-528. DR PDB; 5LZ6; X-ray; 2.60 A; A=364-528. DR PDB; 5TDQ; X-ray; 2.49 A; A=367-528. DR PDB; 6HLN; X-ray; 2.10 A; A=364-528. DR PDB; 6HLT; X-ray; 2.81 A; A/C=364-528. DR PDB; 6HLV; X-ray; 2.50 A; A=364-528. DR PDB; 6HLW; X-ray; 2.73 A; A/C=364-528. DR PDB; 6HM8; X-ray; 2.28 A; A=364-528. DR PDB; 6HMV; X-ray; 2.24 A; A=364-528. DR PDBsum; 2N72; -. DR PDBsum; 2N73; -. DR PDBsum; 5LZ1; -. DR PDBsum; 5LZ3; -. DR PDBsum; 5LZ6; -. DR PDBsum; 5TDQ; -. DR PDBsum; 6HLN; -. DR PDBsum; 6HLT; -. DR PDBsum; 6HLV; -. DR PDBsum; 6HLW; -. DR PDBsum; 6HM8; -. DR PDBsum; 6HMV; -. DR AlphaFoldDB; Q9H3P7; -. DR SMR; Q9H3P7; -. DR BioGRID; 122262; 251. DR DIP; DIP-40673N; -. DR IntAct; Q9H3P7; 92. DR MINT; Q9H3P7; -. DR STRING; 9606.ENSP00000355777; -. DR TCDB; 9.B.17.2.3; the vamp-associated protein (vap) family. DR GlyGen; Q9H3P7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H3P7; -. DR MetOSite; Q9H3P7; -. DR PhosphoSitePlus; Q9H3P7; -. DR SwissPalm; Q9H3P7; -. DR BioMuta; ACBD3; -. DR DMDM; 51316096; -. DR EPD; Q9H3P7; -. DR jPOST; Q9H3P7; -. DR MassIVE; Q9H3P7; -. DR MaxQB; Q9H3P7; -. DR PaxDb; 9606-ENSP00000355777; -. DR PeptideAtlas; Q9H3P7; -. DR ProteomicsDB; 80738; -. DR Pumba; Q9H3P7; -. DR Antibodypedia; 2875; 443 antibodies from 29 providers. DR DNASU; 64746; -. DR Ensembl; ENST00000366812.6; ENSP00000355777.5; ENSG00000182827.9. DR GeneID; 64746; -. DR KEGG; hsa:64746; -. DR MANE-Select; ENST00000366812.6; ENSP00000355777.5; NM_022735.4; NP_073572.2. DR UCSC; uc001hpy.4; human. DR AGR; HGNC:15453; -. DR CTD; 64746; -. DR DisGeNET; 64746; -. DR GeneCards; ACBD3; -. DR HGNC; HGNC:15453; ACBD3. DR HPA; ENSG00000182827; Low tissue specificity. DR MIM; 606809; gene. DR neXtProt; NX_Q9H3P7; -. DR OpenTargets; ENSG00000182827; -. DR PharmGKB; PA28803; -. DR VEuPathDB; HostDB:ENSG00000182827; -. DR eggNOG; KOG3878; Eukaryota. DR GeneTree; ENSGT00530000063651; -. DR HOGENOM; CLU_048443_0_0_1; -. DR InParanoid; Q9H3P7; -. DR OMA; SYSIWRS; -. DR OrthoDB; 2909903at2759; -. DR PhylomeDB; Q9H3P7; -. DR TreeFam; TF321667; -. DR PathwayCommons; Q9H3P7; -. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR SignaLink; Q9H3P7; -. DR BioGRID-ORCS; 64746; 23 hits in 1164 CRISPR screens. DR ChiTaRS; ACBD3; human. DR GeneWiki; ACBD3; -. DR GenomeRNAi; 64746; -. DR Pharos; Q9H3P7; Tbio. DR PRO; PR:Q9H3P7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9H3P7; Protein. DR Bgee; ENSG00000182827; Expressed in tibia and 211 other cell types or tissues. DR ExpressionAtlas; Q9H3P7; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro. DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 2.60.120.680; GOLD domain; 1. DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS. DR InterPro; IPR000582; Acyl-CoA-binding_protein. DR InterPro; IPR035984; Acyl-CoA-binding_sf. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR009038; GOLD_dom. DR InterPro; IPR036598; GOLD_dom_sf. DR PANTHER; PTHR22973:SF11; GOLGI RESIDENT PROTEIN GCP60; 1. DR PANTHER; PTHR22973; LD35087P; 1. DR Pfam; PF00887; ACBP; 1. DR Pfam; PF13897; GOLD_2; 1. DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1. DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1. DR PROSITE; PS00880; ACB_1; 1. DR PROSITE; PS51228; ACB_2; 1. DR PROSITE; PS50866; GOLD; 1. DR Genevisible; Q9H3P7; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing; KW Golgi apparatus; Host-virus interaction; Lipid biosynthesis; KW Lipid metabolism; Membrane; Mitochondrion; Phosphoprotein; KW Reference proteome; Steroid biosynthesis. FT CHAIN 1..528 FT /note="Golgi resident protein GCP60" FT /id="PRO_0000436449" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..528 FT /note="Golgi resident protein GCP60, N-terminally FT processed" FT /id="PRO_0000214029" FT DOMAIN 83..174 FT /note="ACB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573" FT DOMAIN 384..526 FT /note="GOLD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 182..240 FT /note="Charged amino-acid region (CAR)" FT /evidence="ECO:0000269|PubMed:23572552" FT REGION 182..230 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 241..308 FT /note="Q domain; Interaction with PI4KB, TBC1D22A and FT TBC1D22B" FT /evidence="ECO:0000269|PubMed:23572552, FT ECO:0000269|PubMed:27009356" FT REGION 335..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 514..516 FT /note="Membrane-binding" FT /evidence="ECO:0000269|PubMed:28065508, FT ECO:0000269|PubMed:31381608" FT COILED 174..257 FT /evidence="ECO:0000255" FT COMPBIAS 30..48 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 399 FT /note="Membrane-binding" FT /evidence="ECO:0000269|PubMed:28065508, FT ECO:0000269|PubMed:31381608" FT MOD_RES 2 FT /note="N-acetylalanine; in Golgi resident protein GCP60, N- FT terminally processed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 18 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 43 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:24275569" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 187 FT /note="E -> D (in dbSNP:rs2306120)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2" FT /id="VAR_019615" FT MUTAGEN 243 FT /note="K->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 244 FT /note="Q->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 245 FT /note="Q->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 246 FT /note="I->A: Partial loss of PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 253 FT /note="Q->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 254 FT /note="T->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 256..258 FT /note="VQF->AAA: Loss of PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 257 FT /note="Q->A: Partial loss of PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 258..259 FT /note="FQ->AA: Complete loss of interaction with PI4KB." FT /evidence="ECO:0000269|PubMed:27989622" FT MUTAGEN 258..259 FT /note="FQ->AA: Loss of interaction with PI4KB." FT /evidence="ECO:0000269|PubMed:27989622" FT MUTAGEN 258 FT /note="F->A: Differential effect on PI4KB- and FT TBC1D22B-binding, with PI4KB-binding being much more FT affected than TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552, FT ECO:0000269|PubMed:27009356" FT MUTAGEN 259 FT /note="Q->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 260 FT /note="Q->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 261 FT /note="Y->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 264..266 FT /note="QQY->AAA: No effect on PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 266 FT /note="Y->A: No loss of interaction with PI4KB." FT /evidence="ECO:0000269|PubMed:27009356" FT MUTAGEN 267..269 FT /note="PGN->AAA: Loss of PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 275 FT /note="I->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 276 FT /note="L->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 282..285 FT /note="EQHY->AAAA: Loss of PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 284 FT /note="H->A: Almost complete loss of PI4KB- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552, FT ECO:0000269|PubMed:27009356" FT MUTAGEN 285 FT /note="Y->A: Differential loss of PI4KB- and FT TBC1D22B-binding, with PI4KB-binding being much more FT affected than TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552, FT ECO:0000269|PubMed:27009356" FT MUTAGEN 286 FT /note="Q->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 287 FT /note="Q->A: No effect on PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 288 FT /note="Y->A: Almost complete loss of PI4KB- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552, FT ECO:0000269|PubMed:27009356" FT MUTAGEN 344..345 FT /note="SS->AA: No effect on PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 375..377 FT /note="WTR->ATA: 80% reduced ability to interact with the FT 3A protein of enterovirus D68." FT /evidence="ECO:0000269|PubMed:31381608" FT MUTAGEN 380..381 FT /note="IK->AE: No effect on interaction with PI4KB but loss FT of interaction with Kobuviral (Aichi) 3A protein. Loss of FT ability to sensitize PI4KB activation by Kobuviral (Aichi) FT 3A protein." FT /evidence="ECO:0000269|PubMed:27989622" FT MUTAGEN 403..407 FT /note="VTVRV->AAAAA: 95% reduced ability to interact with FT the 3A protein of enterovirus D68." FT /evidence="ECO:0000269|PubMed:31381608" FT MUTAGEN 414..417 FT /note="SYLF->AAAA: 60% reduced ability to interact with the FT 3A protein of enterovirus D68." FT /evidence="ECO:0000269|PubMed:31381608" FT MUTAGEN 414..416 FT /note="SYL->AAA: No effect on PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 417..420 FT /note="FWEF->AAAA: No effect on PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 433..435 FT /note="FEW->AAA: No effect on PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 494..496 FT /note="GSH->AAA: No effect on PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 511..513 FT /note="SYS->AAA: No effect on PI4KB-, TBC1D22A- and FT TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 511 FT /note="S->A: Partial loss of PI4KB- and TBC1D22B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 514..516 FT /note="LWR->AAA: Almost complete loss of Golgi FT loalization." FT /evidence="ECO:0000269|PubMed:31381608" FT MUTAGEN 523..527 FT /note="RVYYT->AAAAA: 75% reduced ability to interact with FT the 3A protein of enterovirus D68." FT /evidence="ECO:0000269|PubMed:31381608" FT MUTAGEN 525 FT /note="Y->A: No effect on interaction with PI4KB but loss FT of interaction with Kobuviral (Aichi) 3A protein. Loss of FT ability to sensitize PI4KB activation by Kobuviral (Aichi) FT 3A protein." FT /evidence="ECO:0000269|PubMed:27989622" FT CONFLICT 93 FT /note="F -> L (in Ref. 2; AAN60219)" FT /evidence="ECO:0000305" FT CONFLICT 230 FT /note="R -> I (in Ref. 2; AAN60219)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="Q -> R (in Ref. 2; AAN60219)" FT /evidence="ECO:0000305" FT CONFLICT 333 FT /note="S -> P (in Ref. 2; AAN60219)" FT /evidence="ECO:0000305" FT CONFLICT 384..397 FT /note="KEKIQQDADSVITV -> QREDSAGCRFRDYS (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 425 FT /note="Y -> C (in Ref. 2; AAN60219)" FT /evidence="ECO:0000305" FT CONFLICT 473 FT /note="K -> R (in Ref. 6; AAH60792)" FT /evidence="ECO:0000305" FT HELIX 243..265 FT /evidence="ECO:0007829|PDB:2N72" FT HELIX 270..304 FT /evidence="ECO:0007829|PDB:2N72" FT STRAND 373..378 FT /evidence="ECO:0007829|PDB:5LZ1" FT HELIX 380..387 FT /evidence="ECO:0007829|PDB:5LZ1" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 402..408 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 414..421 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 423..425 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 427..434 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 444..448 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 476..485 FT /evidence="ECO:0007829|PDB:5LZ1" FT TURN 487..489 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 490..497 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 503..509 FT /evidence="ECO:0007829|PDB:5LZ1" FT STRAND 518..527 FT /evidence="ECO:0007829|PDB:5LZ1" SQ SEQUENCE 528 AA; 60593 MW; B36EC550F8268FC2 CRC64; MAAVLNAERL EVSVDGLTLS PDPEERPGAE GAPLLPPPLP PPSPPGSGRG PGASGEQPEP GEAAAGGAAE EARRLEQRWG FGLEELYGLA LRFFKEKDGK AFHPTYEEKL KLVALHKQVL MGPYNPDTCP EVGFFDVLGN DRRREWAALG NMSKEDAMVE FVKLLNRCCH LFSTYVASHK IEKEEQEKKR KEEEERRRRE EEERERLQKE EEKRRREEEE RLRREEEERR RIEEERLRLE QQKQQIMAAL NSQTAVQFQQ YAAQQYPGNY EQQQILIRQL QEQHYQQYMQ QLYQVQLAQQ QAALQKQQEV VVAGSSLPTS SKVNATVPSN MMSVNGQAKT HTDSSEKELE PEAAEEALEN GPKESLPVIA APSMWTRPQI KDFKEKIQQD ADSVITVGRG EVVTVRVPTH EEGSYLFWEF ATDNYDIGFG VYFEWTDSPN TAVSVHVSES SDDDEEEEEN IGCEEKAKKN ANKPLLDEIV PVYRRDCHEE VYAGSHQYPG RGVYLLKFDN SYSLWRSKSV YYRVYYTR //