GCP60_HUMAN
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 03-AUG-2022, entry version 170.
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 -!- 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}.
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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; 156.
DR DIP; DIP-40673N; -.
DR IntAct; Q9H3P7; 60.
DR MINT; Q9H3P7; -.
DR STRING; 9606.ENSP00000355777; -.
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; Q9H3P7; -.
DR PeptideAtlas; Q9H3P7; -.
DR PRIDE; Q9H3P7; -.
DR ProteomicsDB; 80738; -.
DR Antibodypedia; 2875; 410 antibodies from 28 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 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; NEVYVGS; -.
DR OrthoDB; 733463at2759; -.
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; 21 hits in 1080 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 209 other tissues.
DR ExpressionAtlas; Q9H3P7; baseline and differential.
DR Genevisible; Q9H3P7; HS.
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 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 Pfam; PF00887; ACBP; 1.
DR Pfam; PF13897; GOLD_2; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50866; GOLD; 1.
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 TBC1D22B-
FT 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 TBC1D22B-
FT binding, with PI4KB-binding being much more affected than
FT 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 TBC1D22B-
FT 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 TBC1D22B-
FT binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 284
FT /note="H->A: Almost complete loss of PI4KB- and TBC1D22B-
FT binding."
FT /evidence="ECO:0000269|PubMed:23572552,
FT ECO:0000269|PubMed:27009356"
FT MUTAGEN 285
FT /note="Y->A: Differential loss of PI4KB- and TBC1D22B-
FT binding, with PI4KB-binding being much more affected than
FT 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 TBC1D22B-
FT 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 TBC1D22B-
FT 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
