VDAC2_MOUSE
ID VDAC2_MOUSE Reviewed; 295 AA.
AC Q60930; Q78MH6; Q99L98;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Voltage-dependent anion-selective channel protein 2;
DE Short=VDAC-2;
DE Short=mVDAC2;
DE AltName: Full=Outer mitochondrial membrane protein porin 2;
DE AltName: Full=Voltage-dependent anion-selective channel protein 6;
DE Short=VDAC-6;
DE Short=mVDAC6;
GN Name=Vdac2; Synonyms=Vdac6;
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 TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8660977; DOI=10.1006/geno.1996.0193;
RA Sampson M.J., Lovell R.S., Craigen W.J.;
RT "Isolation, characterization, and mapping of two mouse mitochondrial
RT voltage-dependent anion channel isoforms.";
RL Genomics 33:283-288(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow;
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;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 33-40; 47-65; 76-121; 179-230 AND 237-278, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY 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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KLC3.
RX PubMed=22561200; DOI=10.1016/j.ydbio.2012.04.026;
RA Zhang Y., Ou Y., Cheng M., Saadi H.S., Thundathil J.C., van der Hoorn F.A.;
RT "KLC3 is involved in sperm tail midpiece formation and sperm function.";
RL Dev. Biol. 366:101-110(2012).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-32, AND IDENTIFICATION BY MASS
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [10]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SPATA33.
RX PubMed=33087875; DOI=10.1038/s41418-020-00638-2;
RA Zhang Y., Xu X., Hu M., Wang X., Cheng H., Zhou R.;
RT "SPATA33 is an autophagy mediator for cargo selectivity in germline
RT mitophagy.";
RL Cell Death Differ. 28:1076-1090(2021).
RN [11]
RP INTERACTION WITH ARMC12.
RX PubMed=33536340; DOI=10.1073/pnas.2018355118;
RA Shimada K., Park S., Miyata H., Yu Z., Morohoshi A., Oura S., Matzuk M.M.,
RA Ikawa M.;
RT "ARMC12 regulates spatiotemporal mitochondrial dynamics during
RT spermiogenesis and is required for male fertility.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [12]
RP INTERACTION WITH SPATA33 AND PPP3CC.
RX PubMed=34446558; DOI=10.1073/pnas.2106673118;
RA Miyata H., Oura S., Morohoshi A., Shimada K., Mashiko D., Oyama Y.,
RA Kaneda Y., Matsumura T., Abbasi F., Ikawa M.;
RT "SPATA33 localizes calcineurin to the mitochondria and regulates sperm
RT motility in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane that
CC allows diffusion of small hydrophilic molecules (By similarity). The
CC channel adopts an open conformation at low or zero membrane potential
CC and a closed conformation at potentials above 30-40 mV (By similarity).
CC The open state has a weak anion selectivity whereas the closed state is
CC cation-selective (By similarity). Binds various lipids, including the
CC sphingolipid ceramide, the phospholipid phosphatidylcholine, and the
CC sterol cholesterol (By similarity). Binding of ceramide promotes the
CC Binding of ceramide promotes the mitochondrial outer membrane
CC permeabilization (MOMP) apoptotic pathway (By similarity).
CC {ECO:0000250|UniProtKB:P45880}.
CC -!- SUBUNIT: Interacts with hexokinases (By similarity). Interacts with
CC ARMC12 in a TBC1D21-dependent manner (PubMed:33536340). Interacts with
CC KLC3 (PubMed:22561200). Interacts with SPATA33 (PubMed:34446558,
CC PubMed:33087875). Interacts with PPP3CC in a SPATA33-dependent manner
CC (PubMed:34446558). {ECO:0000250|UniProtKB:P21796,
CC ECO:0000269|PubMed:22561200, ECO:0000269|PubMed:33087875,
CC ECO:0000269|PubMed:33536340, ECO:0000269|PubMed:34446558}.
CC -!- INTERACTION:
CC Q60930; O08734: Bak1; NbExp=3; IntAct=EBI-444578, EBI-822441;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:22561200}. Membrane {ECO:0000250|UniProtKB:P45880}.
CC Note=May localize to non-mitochondrial membranes.
CC {ECO:0000250|UniProtKB:P45880}.
CC -!- TISSUE SPECIFICITY: Highest levels of expression detected in testis,
CC less but still abundant expression in heart, kidney, brain, and
CC skeletal muscle (PubMed:8660977). Expressed in the sperm midpiece (at
CC protein level) (PubMed:33087875). {ECO:0000269|PubMed:33087875,
CC ECO:0000269|PubMed:8660977}.
CC -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19
CC beta-strands. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000250|UniProtKB:P45880}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
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DR EMBL; U30838; AAC13321.1; -; mRNA.
DR EMBL; AK168199; BAE40159.1; -; mRNA.
DR EMBL; AK159561; BAE35185.1; -; mRNA.
DR EMBL; AK152274; BAE31090.1; -; mRNA.
DR EMBL; AK150940; BAE29975.1; -; mRNA.
DR EMBL; AK150627; BAE29717.1; -; mRNA.
DR EMBL; AK150504; BAE29617.1; -; mRNA.
DR EMBL; AK012359; BAE43231.1; -; mRNA.
DR EMBL; AY294423; AAQ01516.1; -; Genomic_DNA.
DR EMBL; BC003731; AAH03731.2; -; mRNA.
DR CCDS; CCDS26867.1; -.
DR RefSeq; NP_035825.1; NM_011695.2.
DR AlphaFoldDB; Q60930; -.
DR SMR; Q60930; -.
DR BioGRID; 204508; 32.
DR IntAct; Q60930; 28.
DR MINT; Q60930; -.
DR STRING; 10090.ENSMUSP00000022293; -.
DR iPTMnet; Q60930; -.
DR PhosphoSitePlus; Q60930; -.
DR SwissPalm; Q60930; -.
DR REPRODUCTION-2DPAGE; Q60930; -.
DR EPD; Q60930; -.
DR jPOST; Q60930; -.
DR MaxQB; Q60930; -.
DR PaxDb; Q60930; -.
DR PeptideAtlas; Q60930; -.
DR PRIDE; Q60930; -.
DR ProteomicsDB; 275176; -.
DR Antibodypedia; 29670; 306 antibodies from 32 providers.
DR DNASU; 22334; -.
DR Ensembl; ENSMUST00000022293; ENSMUSP00000022293; ENSMUSG00000021771.
DR GeneID; 22334; -.
DR KEGG; mmu:22334; -.
DR UCSC; uc007sls.1; mouse.
DR CTD; 7417; -.
DR MGI; MGI:106915; Vdac2.
DR VEuPathDB; HostDB:ENSMUSG00000021771; -.
DR eggNOG; KOG3126; Eukaryota.
DR GeneTree; ENSGT00950000182869; -.
DR InParanoid; Q60930; -.
DR OMA; PWSWRLN; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; Q60930; -.
DR TreeFam; TF315091; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 22334; 17 hits in 57 CRISPR screens.
DR ChiTaRS; Vdac2; mouse.
DR PRO; PR:Q60930; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q60930; protein.
DR Bgee; ENSMUSG00000021771; Expressed in epithelium of stomach and 274 other tissues.
DR ExpressionAtlas; Q60930; baseline and differential.
DR Genevisible; Q60930; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0097001; F:ceramide binding; ISS:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:UniProtKB.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0008308; F:voltage-gated anion channel activity; ISO:MGI.
DR GO; GO:0006820; P:anion transport; ISO:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:MGI.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0032272; P:negative regulation of protein polymerization; IMP:UniProtKB.
DR CDD; cd07306; Porin3_VDAC; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR001925; Porin_Euk.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR InterPro; IPR030277; VDAC2.
DR PANTHER; PTHR11743; PTHR11743; 1.
DR PANTHER; PTHR11743:SF12; PTHR11743:SF12; 1.
DR Pfam; PF01459; Porin_3; 1.
DR PRINTS; PR00185; EUKARYTPORIN.
DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Ion transport; Isopeptide bond;
KW Lipid-binding; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD;
KW Nucleotide-binding; Phosphoprotein; Porin; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport; Ubl conjugation.
FT CHAIN 1..295
FT /note="Voltage-dependent anion-selective channel protein 2"
FT /id="PRO_0000050506"
FT TRANSMEM 38..45
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 51..60
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 66..76
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 81..88
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 92..100
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 107..116
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 122..131
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 135..144
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 148..157
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 161..170
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 177..187
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 190..197
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 201..210
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 214..222
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 229..238
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 243..250
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 254..263
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 267..275
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT TRANSMEM 285..295
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT BINDING 254..256
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 272..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT SITE 85
FT /note="Involved in ceramide and phosphatidylcholine
FT binding"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 79
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 121
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 278
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CONFLICT 260
FT /note="T -> A (in Ref. 4; AAH03731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 31733 MW; 7BBCDC625AD013C7 CRC64;
MAECCVPVCP RPMCIPPPYA DLGKAARDIF NKGFGFGLVK LDVKTKSCSG VEFSTSGSSN
TDTGKVSGTL ETKYKWCEYG LTFTEKWNTD NTLGTEIAIE DQICQGLKLT FDTTFSPNTG
KKSGKIKSAY KRECINLGCD VDFDFAGPAI HGSAVFGYEG WLAGYQMTFD SAKSKLTRSN
FAVGYRTGDF QLHTNVNNGT EFGGSIYQKV CEDFDTSVNL AWTSGTNCTR FGIAAKYQLD
PTASISAKVN NSSLIGVGYT QTLRPGVKLT LSALVDGKSF NAGGHKLGLA LELEA
