TERA_MOUSE
ID TERA_MOUSE Reviewed; 806 AA.
AC Q01853; Q3TFH9; Q3TIM2; Q3TXN9; Q6PI18; Q8BSR6; Q8CEG4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Transitional endoplasmic reticulum ATPase;
DE Short=TER ATPase;
DE EC=3.6.4.6 {ECO:0000250|UniProtKB:P55072};
DE AltName: Full=15S Mg(2+)-ATPase p97 subunit;
DE AltName: Full=Valosin-containing protein;
DE Short=VCP;
GN Name=Vcp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-40; 295-309 AND
RP 425-438.
RC STRAIN=MRL/LPR;
RX PubMed=1382975; DOI=10.1002/j.1460-2075.1992.tb05436.x;
RA Egerton M., Ashe O.R., Chen D., Druker B.J., Burgess W.H., Samelson L.E.;
RT "VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in
RT response to T cell antigen receptor activation.";
RL EMBO J. 11:3533-3540(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow, Head, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 9-18; 26-53; 87-93; 96-109; 148-155; 192-210; 218-231;
RP 240-251; 278-287; 296-312; 324-336; 363-386; 454-502; 513-524; 530-560;
RP 600-614; 639-651; 669-677; 701-709; 714-732 AND 754-766, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH UBOX5.
RX PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
RA Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
RT "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular
RT chaperones.";
RL Genes Cells 9:533-548(2004).
RN [7]
RP INTERACTION WITH RNF19A.
RX PubMed=15456787; DOI=10.1074/jbc.m406683200;
RA Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S.,
RA Kakizuka A., Tanaka K., Sobue G.;
RT "Physical and functional interaction between dorfin and valosin-containing
RT protein that are colocalized in ubiquitylated inclusions in
RT neurodegenerative disorders.";
RL J. Biol. Chem. 279:51376-51385(2004).
RN [8]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-805, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP INTERACTION WITH NGLY1.
RX PubMed=16249333; DOI=10.1073/pnas.0507155102;
RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.;
RT "Multiple modes of interaction of the deglycosylation enzyme, mouse peptide
RT N-glycanase, with the proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005).
RN [11]
RP ERRATUM OF PUBMED:16249333.
RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006).
RN [12]
RP INTERACTION WITH NSFL1C-LIKE PROTEIN P37.
RX PubMed=17141156; DOI=10.1016/j.devcel.2006.10.016;
RA Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E., Dreveny I.,
RA Beuron F., Zhang X., Freemont P., Kondo H.;
RT "p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase
RT and at the end of mitosis.";
RL Dev. Cell 11:803-816(2006).
RN [13]
RP PHOSPHOLIPID BINDING, AND MUTAGENESIS OF ARG-144.
RX PubMed=17018057; DOI=10.1111/j.1742-4658.2006.05494.x;
RA Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N., Shimozawa N.,
RA Shirakawa M., Hiroaki H.;
RT "The common phospholipid-binding activity of the N-terminal domains of PEX1
RT and VCP/p97.";
RL FEBS J. 273:4959-4971(2006).
RN [14]
RP INTERACTION WITH AMFR; SAKS1; RAD23B AND NGLY1.
RX PubMed=16709668; DOI=10.1073/pnas.0602747103;
RA Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.;
RT "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-
RT associated E3 ligase autocrine motility factor receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP METHYLATION AT LYS-315.
RX PubMed=22948820; DOI=10.1038/ncomms2041;
RA Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
RA Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
RT "Lysine methylation of VCP by a member of a novel human protein
RT methyltransferase family.";
RL Nat. Commun. 3:1038-1038(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-502; LYS-505; LYS-668 AND
RP LYS-754, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-668, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [18]
RP INTERACTION WITH ZFAND2B.
RX PubMed=24160817; DOI=10.1042/bj20130710;
RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA Edelmann M.J., Kessler B.M., Stanhill A.;
RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT complex.";
RL Biochem. J. 457:253-261(2014).
RN [19]
RP INTERACTION WITH CCDC47.
RX PubMed=25009997; DOI=10.1016/j.ydbio.2014.06.024;
RA Yamamoto S., Yamazaki T., Komazaki S., Yamashita T., Osaki M.,
RA Matsubayashi M., Kidoya H., Takakura N., Yamazaki D., Kakizawa S.;
RT "Contribution of calumin to embryogenesis through participation in the
RT endoplasmic reticulum-associated degradation activity.";
RL Dev. Biol. 393:33-43(2014).
RN [20]
RP INTERACTION WITH ZFAND2B.
RX PubMed=26337389; DOI=10.1091/mbc.e15-02-0085;
RA Braunstein I., Zach L., Allan S., Kalies K.U., Stanhill A.;
RT "Proteasomal degradation of preemptive quality control (pQC) substrates is
RT mediated by an AIRAPL-p97 complex.";
RL Mol. Biol. Cell 26:3719-3727(2015).
RN [21]
RP INTERACTION WITH LMBR1L AND UBAC2.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-458 IN COMPLEX WITH ADP.
RX PubMed=11163219; DOI=10.1016/s1097-2765(00)00143-x;
RA Zhang X., Shaw A., Bates P.A., Newman R.H., Gowen B., Orlova E.,
RA Gorman M.A., Kondo H., Dokurno P., Lally J., Leonard G., Meyer H.,
RA van Heel M., Freemont P.S.;
RT "Structure of the AAA ATPase p97.";
RL Mol. Cell 6:1473-1484(2000).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (4.7 ANGSTROMS).
RX PubMed=12949490; DOI=10.1038/nsb972;
RA DeLaBarre B., Brunger A.T.;
RT "Complete structure of p97/valosin-containing protein reveals communication
RT between nucleotide domains.";
RL Nat. Struct. Biol. 10:856-863(2003).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
RX PubMed=14643202; DOI=10.1016/j.jsb.2003.10.007;
RA Huyton T., Pye V.E., Briggs L.C., Flynn T.C., Beuron F., Kondo H., Ma J.,
RA Zhang X., Freemont P.S.;
RT "The crystal structure of murine p97/VCP at 3.6A.";
RL J. Struct. Biol. 144:337-348(2003).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-458 IN COMPLEX WITH ADP.
RX PubMed=14988733; DOI=10.1038/sj.emboj.7600139;
RA Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.;
RT "Structural basis of the interaction between the AAA ATPase p97/VCP and its
RT adaptor protein p47.";
RL EMBO J. 23:1030-1039(2004).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=15740751; DOI=10.1016/j.jmb.2005.01.060;
RA DeLaBarre B., Brunger A.T.;
RT "Nucleotide dependent motion and mechanism of action of p97/VCP.";
RL J. Mol. Biol. 347:437-452(2005).
CC -!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
CC mitosis and for their reassembly after mitosis. Involved in the
CC formation of the transitional endoplasmic reticulum (tER). The transfer
CC of membranes from the endoplasmic reticulum to the Golgi apparatus
CC occurs via 50-70 nm transition vesicles which derive from part-rough,
CC part-smooth transitional elements of the endoplasmic reticulum (tER).
CC Vesicle budding from the tER is an ATP-dependent process. The ternary
CC complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins
CC and is necessary for the export of misfolded proteins from the ER to
CC the cytoplasm, where they are degraded by the proteasome. The NPLOC4-
CC UFD1-VCP complex regulates spindle disassembly at the end of mitosis
CC and is necessary for the formation of a closed nuclear envelope.
CC Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of
CC the VCP/p97-AMFR/gp78 complex that participates in the final step of
CC the sterol-mediated ubiquitination and endoplasmic reticulum-associated
CC degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-
CC induced pre-emptive quality control, a mechanism that selectively
CC attenuates the translocation of newly synthesized proteins into the
CC endoplasmic reticulum and reroutes them to the cytosol for proteasomal
CC degradation. Plays a role in the regulation of stress granules (SGs)
CC clearance process upon arsenite-induced response (By similarity). Also
CC involved in DNA damage response: recruited to double-strand breaks
CC (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the
CC recruitment of TP53BP1 at DNA damage sites. Recruited to stalled
CC replication forks by SPRTN: may act by mediating extraction of DNA
CC polymerase eta (POLH) to prevent excessive translesion DNA synthesis
CC and limit the incidence of mutations induced by DNA damage. Together
CC with SPRTN metalloprotease, involved in the repair of covalent DNA-
CC protein cross-links (DPCs) during DNA synthesis. Involved in
CC interstrand cross-link repair in response to replication stress by
CC mediating unloading of the ubiquitinated CMG helicase complex. Required
CC for cytoplasmic retrotranslocation of stressed/damaged mitochondrial
CC outer-membrane proteins and their subsequent proteasomal degradation.
CC Essential for the maturation of ubiquitin-containing autophagosomes and
CC the clearance of ubiquitinated protein by autophagy. Acts as a negative
CC regulator of type I interferon production by interacting with
CC DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated
CC via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit
CC RNF125 and promote ubiquitination and degradation of DDX58/RIG-I. May
CC play a role in the ubiquitin-dependent sorting of membrane proteins to
CC lysosomes where they undergo degradation. May more particularly play a
CC role in caveolins sorting in cells. By controlling the steady-state
CC expression of the IGF1R receptor, indirectly regulates the insulin-like
CC growth factor receptor signaling pathway.
CC {ECO:0000250|UniProtKB:P23787, ECO:0000250|UniProtKB:P46462,
CC ECO:0000250|UniProtKB:P55072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000250|UniProtKB:P55072};
CC -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter,
CC that displays 6-fold radial symmetry. Part of a ternary complex
CC containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds
CC to one end of a VCP homohexamer. The complex binds to membranes
CC enriched in phosphatidylethanolamine-containing lipids and promotes
CC Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1,
CC binding to this heterodimer inhibits Golgi-membrane fusion. Interaction
CC with VCIP135 leads to dissociation of the complex via ATP hydrolysis by
CC VCP. Part of a ternary complex containing NPLOC4, UFD1 and VCP.
CC Interacts with NSFL1C-like protein p37; the complex has membrane fusion
CC activity and is required for Golgi and endoplasmic reticulum
CC biogenesis. Interacts with RNF103. Interacts with TRIM13 and TRIM21.
CC Component of a VCP/p97-AMFR/gp78 complex that participates in the final
CC step of the endoplasmic reticulum-associated degradation (ERAD) of
CC HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with
CC RHBDD1 (via C-terminal domain). Interacts with SPRTN; leading to
CC recruitment to stalled replication forks. Interacts with SELENOS and
CC SYVN1, as well as with DERL1 (via SHP-box motif), DERL2 and DERL3;
CC which probably transfer misfolded proteins from the ER to VCP.
CC Interacts with SVIP. Component of a complex required to couple
CC retrotranslocation, ubiquitination and deglycosylation composed of
CC NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXN4 and
CC RNF19A. Interacts with CASR. Interacts with UBE4B and YOD1. Interacts
CC with clathrin. Interacts with RNF103. Interacts with TRIM13 and TRIM21.
CC Component of a VCP/p97-AMFR/gp78 complex that participates in the final
CC step of the endoplasmic reticulum-associated degradation (ERAD) of
CC HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with
CC WASHC5. Interacts with UBOX5. Interacts (via N- terminus) with UBXN7,
CC UBXN8, and probably several other UBX domain-containing proteins (via
CC UBX domains); the interactions are mutually exclusive with VIM-
CC dependent interactions such as those with AMFR and SELENOS. Forms a
CC complex with UBQLN1 and UBXN4 (By similarity). Interacts (via the PIM
CC motif) with RNF31 (via the PUB domain) (By similarity). Interacts with
CC DDX58/RIG-I and RNF125; interaction takes place when DDX58/RIG-I is
CC ubiquitinated via'Lys-63'-linked ubiquitin on its CARD domains, leading
CC to recruit RNF125 and promote ubiquitination and degradation of
CC DDX58/RIG-I (By similarity). Interacts with BAG6 (By similarity).
CC Interacts with UBXN10 (By similarity). Interacts with UBXN6; the
CC interaction with UBXN6 is direct and competitive with UFD1 (By
CC similarity). Forms a ternary complex with CAV1 and UBXN6. Interacts
CC with PLAA, UBXN6 and YOD1; may form a complex involved in
CC macroautophagy (By similarity). Interacts with ANKZF1 (By similarity).
CC Interacts with ubiquitin-binding protein FAF1 (By similarity).
CC Interacts with ZFAND2B (via VIM motif); the interaction is direct
CC (PubMed:24160817, PubMed:26337389). Interacts with ZFAND1 (via its
CC ubiquitin-like region); this interaction occurs in an arsenite-
CC dependent manner (By similarity). Interacts with CCDC47
CC (PubMed:25009997). Interacts with LMBR1L and UBAC2 (PubMed:31073040).
CC Interacts with ATXN3 (By similarity). Interacts with TEX264; bridging
CC VCP to covalent DNA-protein cross-links (DPCs) (By similarity).
CC {ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072,
CC ECO:0000269|PubMed:15189447, ECO:0000269|PubMed:15456787,
CC ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16709668,
CC ECO:0000269|PubMed:17141156, ECO:0000269|PubMed:24160817,
CC ECO:0000269|PubMed:25009997, ECO:0000269|PubMed:26337389,
CC ECO:0000269|PubMed:31073040}.
CC -!- INTERACTION:
CC Q01853; Q9R049: Amfr; NbExp=4; IntAct=EBI-80597, EBI-3648125;
CC Q01853; Q80UU1: Ankzf1; NbExp=2; IntAct=EBI-80597, EBI-9510971;
CC Q01853; Q9JI78: Ngly1; NbExp=9; IntAct=EBI-80597, EBI-3648128;
CC Q01853; P70362: Ufd1; NbExp=9; IntAct=EBI-80597, EBI-7961331;
CC Q01853; Q01853: Vcp; NbExp=3; IntAct=EBI-80597, EBI-80597;
CC Q01853; P36037: DOA1; Xeno; NbExp=2; IntAct=EBI-80597, EBI-6017;
CC Q01853; Q9ES54: Nploc4; Xeno; NbExp=11; IntAct=EBI-80597, EBI-1993990;
CC Q01853; O35987: Nsfl1c; Xeno; NbExp=8; IntAct=EBI-80597, EBI-1993760;
CC Q01853; Q9BQE4: SELENOS; Xeno; NbExp=4; IntAct=EBI-80597, EBI-398970;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P55072}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}.
CC Note=Recruited to the cytoplasmic surface of the endoplasmic reticulum
CC via interaction with AMFR/gp78. Following DNA double-strand breaks,
CC recruited to the sites of damage. Recruited to stalled replication
CC forks via interaction with SPRTN. Recruited to damaged lysosomes
CC decorated with K48-linked ubiquitin chains. Colocalizes with TIA1,
CC ZFAND1 and G3BP1 in cytoplasmic stress granules (SGs) in response to
CC arsenite-induced stress treatment (By similarity).
CC {ECO:0000250|UniProtKB:P55072}.
CC -!- DOMAIN: The N-terminal domain shows evolutionary conservation with that
CC of PEX1, and is able to bind phospholipids with a preference for
CC phosphatidylinositol mono- and bisphosphates.
CC -!- DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction with
CC the PUB domain of RNF31. {ECO:0000250|UniProtKB:P55072}.
CC -!- PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen
CC receptor activation. Phosphorylated in mitotic cells.
CC {ECO:0000250|UniProtKB:P46462}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in the
CC presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; Z14044; CAA78412.1; -; mRNA.
DR EMBL; AK028264; BAC25849.1; -; mRNA.
DR EMBL; AK030751; BAC27119.1; -; mRNA.
DR EMBL; AK149931; BAE29175.1; -; mRNA.
DR EMBL; AK151109; BAE30119.1; -; mRNA.
DR EMBL; AK151418; BAE30383.1; -; mRNA.
DR EMBL; AK153249; BAE31840.1; -; mRNA.
DR EMBL; AK159177; BAE34876.1; -; mRNA.
DR EMBL; AK159509; BAE35141.1; -; mRNA.
DR EMBL; AK167794; BAE39824.1; -; mRNA.
DR EMBL; AK169140; BAE40919.1; -; mRNA.
DR EMBL; AL672276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043053; AAH43053.1; -; mRNA.
DR EMBL; BC049114; AAH49114.1; -; mRNA.
DR CCDS; CCDS18086.1; -.
DR PIR; S25197; S25197.
DR RefSeq; NP_033529.3; NM_009503.4.
DR PDB; 1E32; X-ray; 2.90 A; A=1-458.
DR PDB; 1R7R; X-ray; 3.60 A; A=1-806.
DR PDB; 1S3S; X-ray; 2.90 A; A/B/C/D/E/F=1-458.
DR PDB; 2PJH; NMR; -; B=21-213.
DR PDB; 3CF0; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=463-763.
DR PDB; 3CF1; X-ray; 4.40 A; A/B/C=1-806.
DR PDB; 3CF2; X-ray; 3.50 A; A/B/C/D=1-806.
DR PDB; 3CF3; X-ray; 4.25 A; A/B/C=1-806.
DR PDBsum; 1E32; -.
DR PDBsum; 1R7R; -.
DR PDBsum; 1S3S; -.
DR PDBsum; 2PJH; -.
DR PDBsum; 3CF0; -.
DR PDBsum; 3CF1; -.
DR PDBsum; 3CF2; -.
DR PDBsum; 3CF3; -.
DR AlphaFoldDB; Q01853; -.
DR SMR; Q01853; -.
DR BioGRID; 234661; 141.
DR ComplexPortal; CPX-136; Vcp-Npl4-Ufd1 AAA ATPase complex.
DR ComplexPortal; CPX-264; Nsfl1c-Vcp complex.
DR CORUM; Q01853; -.
DR DIP; DIP-29796N; -.
DR IntAct; Q01853; 40.
DR MINT; Q01853; -.
DR STRING; 10090.ENSMUSP00000030164; -.
DR BindingDB; Q01853; -.
DR ChEMBL; CHEMBL3988606; -.
DR iPTMnet; Q01853; -.
DR PhosphoSitePlus; Q01853; -.
DR SwissPalm; Q01853; -.
DR REPRODUCTION-2DPAGE; Q01853; -.
DR UCD-2DPAGE; Q01853; -.
DR CPTAC; non-CPTAC-4013; -.
DR EPD; Q01853; -.
DR jPOST; Q01853; -.
DR MaxQB; Q01853; -.
DR PaxDb; Q01853; -.
DR PeptideAtlas; Q01853; -.
DR PRIDE; Q01853; -.
DR ProteomicsDB; 263105; -.
DR Antibodypedia; 2215; 679 antibodies from 43 providers.
DR DNASU; 269523; -.
DR Ensembl; ENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452.
DR GeneID; 269523; -.
DR KEGG; mmu:269523; -.
DR UCSC; uc008sor.2; mouse.
DR CTD; 7415; -.
DR MGI; MGI:99919; Vcp.
DR VEuPathDB; HostDB:ENSMUSG00000028452; -.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00900000141071; -.
DR HOGENOM; CLU_000688_12_3_1; -.
DR InParanoid; Q01853; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; Q01853; -.
DR TreeFam; TF300542; -.
DR Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR Reactome; R-MMU-3371511; HSF1 activation.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5689877; Josephin domain DUBs.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8876725; Protein methylation.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR BioGRID-ORCS; 269523; 35 hits in 109 CRISPR screens.
DR ChiTaRS; Vcp; mouse.
DR EvolutionaryTrace; Q01853; -.
DR PRO; PR:Q01853; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q01853; protein.
DR Bgee; ENSMUSG00000028452; Expressed in hindlimb stylopod muscle and 236 other tissues.
DR Genevisible; Q01853; MM.
DR GO; GO:1904949; C:ATPase complex; IMP:CAFA.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990730; C:VCP-NSFL1C complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043531; F:ADP binding; IMP:CAFA.
DR GO; GO:0005524; F:ATP binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:1904288; F:BAT3 complex binding; ISO:MGI.
DR GO; GO:0035800; F:deubiquitinase activator activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0070842; P:aggresome assembly; IGI:MGI.
DR GO; GO:0046034; P:ATP metabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:MGI.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0072389; P:flavin adenine dinucleotide catabolic process; ISO:MGI.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; ISO:MGI.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; ISO:MGI.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0035617; P:stress granule disassembly; ISS:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:MGI.
DR GO; GO:0019079; P:viral genome replication; ISO:MGI.
DR DisProt; DP00435; -.
DR Gene3D; 3.40.50.300; -; 2.
DR IDEAL; IID50030; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Autophagy; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; Endoplasmic reticulum;
KW Hydrolase; Isopeptide bond; Lipid-binding; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transport; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT CHAIN 2..806
FT /note="Transitional endoplasmic reticulum ATPase"
FT /id="PRO_0000084573"
FT REGION 708..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..806
FT /note="Interaction with UBXN6"
FT /evidence="ECO:0000250"
FT MOTIF 802..806
FT /note="PIM motif"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT COMPBIAS 768..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:11163219,
FT ECO:0000305|PubMed:14988733"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:11163219,
FT ECO:0000305|PubMed:14988733"
FT BINDING 521..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:11163219,
FT ECO:0000305|PubMed:14988733"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 315
FT /note="N6,N6,N6-trimethyllysine; by VCPKMT"
FT /evidence="ECO:0000269|PubMed:22948820"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 502
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 505
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 668
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 668
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 754
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 805
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MUTAGEN 144
FT /note="R->A: Loss of phospholipid-binding."
FT /evidence="ECO:0000269|PubMed:17018057"
FT CONFLICT 73
FT /note="S -> Y (in Ref. 2; BAC27119)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="N -> Y (in Ref. 2; BAE39824)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="I -> V (in Ref. 1; CAA78412)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="R -> Q (in Ref. 2; BAC27119)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="A -> T (in Ref. 2; BAE40919)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="N -> S (in Ref. 2; BAE34876)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="G -> V (in Ref. 2; BAC25849)"
FT /evidence="ECO:0000305"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3CF2"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2PJH"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1E32"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:1E32"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 159..176
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2PJH"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3CF2"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:1E32"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:1S3S"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 408..430
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:1E32"
FT HELIX 449..456
FT /evidence="ECO:0007829|PDB:1E32"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:3CF2"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 483..498
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 500..506
FT /evidence="ECO:0007829|PDB:3CF0"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:3CF0"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:3CF0"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 544..552
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 558..568
FT /evidence="ECO:0007829|PDB:3CF0"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:3CF0"
FT TURN 586..590
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 599..609
FT /evidence="ECO:0007829|PDB:3CF0"
FT STRAND 615..624
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:3CF0"
FT TURN 636..638
FT /evidence="ECO:0007829|PDB:3CF2"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 650..661
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 672..677
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 684..706
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 733..740
FT /evidence="ECO:0007829|PDB:3CF0"
FT HELIX 749..762
FT /evidence="ECO:0007829|PDB:3CF0"
SQ SEQUENCE 806 AA; 89322 MW; 501B721D3A77BA8A CRC64;
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT
VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF
GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN
LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG
AGPSQGSGGG TGGSVYTEDN DDDLYG
