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Transitional endoplasmic reticulum ATPase TER94 (EC 3.6.4.6) (Valosin-containing protein homolog)

 TERA_DROME              Reviewed;         801 AA.
Q7KN62; A8DY85; A8DY86; O76279; Q9U463;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 1.
30-AUG-2017, entry version 122.
RecName: Full=Transitional endoplasmic reticulum ATPase TER94;
EC=3.6.4.6;
AltName: Full=Valosin-containing protein homolog;
Name=TER94; Synonyms=VCP; ORFNames=CG2331;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 163-176;
214-220; 229-245; 294-308; 456-479; 485-499; 503-520; 563-580;
613-632; 666-687; 694-707 AND 740-748, DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
STRAIN=Canton-S;
PubMed=9639875; DOI=10.1016/S0965-1748(97)00095-7;
Pinter M., Jekely G., Szepesi R.J., Farkas A., Theopold U.,
Meyer H.E., Lindholm D., Nassel D.R., Hultmark D., Friedrich P.;
"TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97,
is accumulated in nonproliferating cells: in the reproductive organs
and in the brain of the imago.";
Insect Biochem. Mol. Biol. 28:91-98(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, AND
MUTAGENESIS OF GLU-437.
PubMed=10656772; DOI=10.1006/dbio.1999.9583;
Ruden D.M., Sollars V., Wang X., Mori D., Alterman M., Lu X.;
"Membrane fusion proteins are required for oskar mRNA localization in
the Drosophila egg chamber.";
Dev. Biol. 218:314-325(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Ovary;
PubMed=10731138; DOI=10.1126/science.287.5461.2222;
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E.,
Stapleton M., Harvey D.A.;
"A Drosophila complementary DNA resource.";
Science 287:2222-2224(2000).
[6]
TISSUE SPECIFICITY, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=10564274; DOI=10.1091/mbc.10.11.3825;
Leon A., McKearin D.;
"Identification of TER94, an AAA ATPase protein, as a Bam-dependent
component of the Drosophila fusome.";
Mol. Biol. Cell 10:3825-3834(1999).
[7]
FUNCTION.
PubMed=14657277; DOI=10.1242/jcs.00841;
Wojcik C., Yano M., DeMartino G.N.;
"RNA interference of valosin-containing protein (VCP/p97) reveals
multiple cellular roles linked to ubiquitin/proteasome-dependent
proteolysis.";
J. Cell Sci. 117:281-292(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[9]
FUNCTION, INTERACTION WITH TUD AND VAS, AND SUBCELLULAR LOCATION.
PubMed=18590813; DOI=10.1016/j.mod.2008.06.005;
Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.;
"Isolation of new polar granule components in Drosophila reveals P
body and ER associated proteins.";
Mech. Dev. 125:865-873(2008).
[10]
INTERACTION WITH PAPI AND AGO3.
PubMed=21447556; DOI=10.1242/dev.059287;
Liu L., Qi H., Wang J., Lin H.;
"PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and
TRAL in the nuage to silence transposition.";
Development 138:1863-1873(2011).
[11] {ECO:0000244|PDB:4RV0}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-186 IN COMPLEX WITH NPL4,
AND INTERACTION WITH TER94.
PubMed=26471729; DOI=10.15252/embj.201591888;
Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
"A non-canonical role of the p97 complex in RIG-I antiviral
signaling.";
EMBO J. 34:2903-2920(2015).
-!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
mitosis and for their reassembly after mitosis. Involved in the
formation of the transitional endoplasmic reticulum (tER). The
transfer of membranes from the endoplasmic reticulum to the Golgi
apparatus occurs via 50-70 nm transition vesicles which derive
from part-rough, part-smooth transitional elements of the
endoplasmic reticulum (tER). Vesicle budding from the tER is an
ATP-dependent process. Involved in the ubiquitin-proteasome
system. Important for oskar mRNA localization and/or anchoring
during oogenesis. Involved in germ cell formation.
{ECO:0000269|PubMed:14657277, ECO:0000269|PubMed:18590813}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Homohexamer (PubMed:10564274). Interacts with tud, vas,
papi and AGO3 (PubMed:18590813, PubMed:21447556). Interacts with
Npl4 (PubMed:26471729). {ECO:0000269|PubMed:10564274,
ECO:0000269|PubMed:18590813, ECO:0000269|PubMed:21447556,
ECO:0000269|PubMed:26471729}.
-!- INTERACTION:
A1ZAB3:Ptp52F; NbExp=5; IntAct=EBI-224053, EBI-3410206;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10564274}.
Nucleus {ECO:0000269|PubMed:10564274}. Note=Component of the
meiotic nuage, also named P granule, a germ-cell-specific
organelle required to repress transposon activity during meiosis
(PubMed:18590813). {ECO:0000269|PubMed:18590813}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A;
IsoId=Q7KN62-1; Sequence=Displayed;
Name=D;
IsoId=Q7KN62-2; Sequence=VSP_035052;
Note=No experimental confirmation available.;
Name=C;
IsoId=Q7KN62-3; Sequence=VSP_035053;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Present in the mushroom bodies of the
protocerebrum and in the glomeruli of the antennal lobe. Present
in nurse cells, oocytes and sperm bundles (at protein level).
{ECO:0000269|PubMed:10564274, ECO:0000269|PubMed:10656772,
ECO:0000269|PubMed:9639875}.
-!- DEVELOPMENTAL STAGE: Present in egg, pupa and imago but not larva
(at protein level). {ECO:0000269|PubMed:9639875}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF17568.1; Type=Frameshift; Positions=136, 142, 757, 761; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF047037; AAC27447.1; -; mRNA.
EMBL; AF202034; AAF17568.1; ALT_FRAME; mRNA.
EMBL; AE013599; ABV53745.1; -; Genomic_DNA.
EMBL; AE013599; ABV53746.1; -; Genomic_DNA.
EMBL; AE013599; AAF58863.1; -; Genomic_DNA.
EMBL; AF132553; AAD27852.1; -; mRNA.
RefSeq; NP_001097249.1; NM_001103779.2. [Q7KN62-3]
RefSeq; NP_001097250.1; NM_001103780.2. [Q7KN62-2]
RefSeq; NP_477369.1; NM_058021.4. [Q7KN62-1]
UniGene; Dm.2968; -.
PDB; 4RV0; X-ray; 2.00 A; A/C/E/G=20-186.
PDBsum; 4RV0; -.
ProteinModelPortal; Q7KN62; -.
SMR; Q7KN62; -.
BioGrid; 61868; 80.
DIP; DIP-52184N; -.
IntAct; Q7KN62; 6.
STRING; 7227.FBpp0111818; -.
iPTMnet; Q7KN62; -.
PaxDb; Q7KN62; -.
PRIDE; Q7KN62; -.
EnsemblMetazoa; FBtr0088391; FBpp0087479; FBgn0261014. [Q7KN62-1]
EnsemblMetazoa; FBtr0112905; FBpp0111818; FBgn0261014. [Q7KN62-3]
EnsemblMetazoa; FBtr0112906; FBpp0111819; FBgn0261014. [Q7KN62-2]
GeneID; 36040; -.
KEGG; dme:Dmel_CG2331; -.
UCSC; CG2331-RA; d. melanogaster. [Q7KN62-1]
UCSC; CG2331-RC; d. melanogaster.
UCSC; CG2331-RD; d. melanogaster.
CTD; 36040; -.
FlyBase; FBgn0261014; TER94.
eggNOG; KOG0730; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00890000139420; -.
InParanoid; Q7KN62; -.
KO; K13525; -.
OMA; PIDDTTE; -.
OrthoDB; EOG091G024K; -.
PhylomeDB; Q7KN62; -.
Reactome; R-DME-110320; Translesion Synthesis by POLH.
Reactome; R-DME-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
Reactome; R-DME-5689896; Ovarian tumor domain proteases.
Reactome; R-DME-6798695; Neutrophil degranulation.
GenomeRNAi; 36040; -.
PRO; PR:Q7KN62; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0261014; -.
ExpressionAtlas; Q7KN62; differential.
Genevisible; Q7KN62; DM.
GO; GO:0044754; C:autolysosome; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0045169; C:fusome; IDA:FlyBase.
GO; GO:0031965; C:nuclear membrane; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0043186; C:P granule; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0000502; C:proteasome complex; NAS:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
GO; GO:0098586; P:cellular response to virus; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0016320; P:endoplasmic reticulum membrane fusion; ISS:FlyBase.
GO; GO:0007029; P:endoplasmic reticulum organization; IMP:FlyBase.
GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
GO; GO:0007040; P:lysosome organization; IMP:FlyBase.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
GO; GO:0007279; P:pole cell formation; IGI:FlyBase.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:FlyBase.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IMP:FlyBase.
GO; GO:0006508; P:proteolysis; IMP:FlyBase.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:FlyBase.
GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:FlyBase.
Gene3D; 3.10.330.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR005938; AAA_ATPase_CDC48.
InterPro; IPR009010; Asp_de-COase-like_dom.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR004201; Cdc48_dom2.
InterPro; IPR029067; CDC48_domain_2-like.
InterPro; IPR003338; CDC4_N-term_subdom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 2.
Pfam; PF02933; CDC48_2; 1.
Pfam; PF02359; CDC48_N; 1.
Pfam; PF09336; Vps4_C; 1.
SMART; SM00382; AAA; 2.
SMART; SM01072; CDC48_2; 1.
SMART; SM01073; CDC48_N; 1.
SUPFAM; SSF50692; SSF50692; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54585; SSF54585; 1.
TIGRFAMs; TIGR01243; CDC48; 1.
PROSITE; PS00674; AAA; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Developmental protein; Differentiation;
Direct protein sequencing; Hydrolase; Nucleotide-binding; Nucleus;
Oogenesis; Phosphoprotein; Reference proteome; Transport;
Ubl conjugation pathway.
CHAIN 1 801 Transitional endoplasmic reticulum ATPase
TER94.
/FTId=PRO_0000347178.
NP_BIND 244 250 ATP. {ECO:0000250|UniProtKB:P55072}.
NP_BIND 518 523 ATP. {ECO:0000250|UniProtKB:Q01853}.
BINDING 345 345 ATP. {ECO:0000250|UniProtKB:P55072}.
BINDING 381 381 ATP. {ECO:0000250|UniProtKB:P55072}.
MOD_RES 716 716 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
VAR_SEQ 1 42 Missing (in isoform D). {ECO:0000305}.
/FTId=VSP_035052.
VAR_SEQ 1 6 MADSKG -> MDHDGDTRDFMRGYHSEQDEKMKPKDSFDKR
(in isoform C). {ECO:0000305}.
/FTId=VSP_035053.
MUTAGEN 437 437 E->A: In ter94-26-8; arrests early in
oogenesis. {ECO:0000269|PubMed:10656772}.
CONFLICT 524 524 L -> P (in Ref. 2; AAF17568).
{ECO:0000305}.
CONFLICT 563 564 AR -> GP (in Ref. 2; AAF17568).
{ECO:0000305}.
CONFLICT 582 584 ARG -> SRC (in Ref. 2; AAF17568).
{ECO:0000305}.
CONFLICT 590 591 AG -> C (in Ref. 2; AAF17568).
{ECO:0000305}.
CONFLICT 661 662 SP -> FA (in Ref. 2; AAF17568).
{ECO:0000305}.
CONFLICT 662 662 P -> A (in Ref. 1; AAC27447).
{ECO:0000305}.
CONFLICT 720 720 Missing (in Ref. 2; AAF17568).
{ECO:0000305}.
CONFLICT 735 735 E -> Q (in Ref. 1; AAC27447).
{ECO:0000305}.
STRAND 22 27 {ECO:0000244|PDB:4RV0}.
STRAND 35 38 {ECO:0000244|PDB:4RV0}.
HELIX 40 46 {ECO:0000244|PDB:4RV0}.
STRAND 53 57 {ECO:0000244|PDB:4RV0}.
STRAND 63 70 {ECO:0000244|PDB:4RV0}.
STRAND 78 81 {ECO:0000244|PDB:4RV0}.
HELIX 83 88 {ECO:0000244|PDB:4RV0}.
STRAND 96 101 {ECO:0000244|PDB:4RV0}.
STRAND 109 115 {ECO:0000244|PDB:4RV0}.
HELIX 127 130 {ECO:0000244|PDB:4RV0}.
HELIX 132 136 {ECO:0000244|PDB:4RV0}.
TURN 137 139 {ECO:0000244|PDB:4RV0}.
STRAND 142 144 {ECO:0000244|PDB:4RV0}.
STRAND 148 153 {ECO:0000244|PDB:4RV0}.
STRAND 156 172 {ECO:0000244|PDB:4RV0}.
STRAND 178 180 {ECO:0000244|PDB:4RV0}.
SEQUENCE 801 AA; 88859 MW; ECF8F173B3B10B07 CRC64;
MADSKGEDLA TAILKRKDRP NRLIVEEAQN DDNSVVSLSQ AKMDELQLFR GDTVILKGKR
RKETVCIVLS DDTCPDEKIR MNRVVRNNLC VHLSDVVSVQ SCPDVKYGKR VRILPIDEST
EGVTGNLFEI YLKPYFLEAY RPIHMGDNFI VRAAMRPIEF KVVLTDPEPY CIVAPETVIF
CDGDPIKREE EEESLNAVGY DDIGGCRKQL AQIKEMVELP LRHPSLFKAI GVKPPRGILM
YGPPGTGKTL IARAVANETG AFFFLINGPE IMSKLAGESE SNLRKAFEEA EKNSPAIIFI
DEIDAIAPKR DKTHGEVERR IVSQLLTLMD GMKKSSHLIV MAATNRPNSI DPALRRFGRF
DREIDIGIPD ATGRLEVLRI HTKNMKLHDD VDLEQIAAES HGHVGADLAS LCSEAALQQI
REKMDLIDLE DDKIDAEVLA SLAVTMENFR YAMTKSSPSA LRETVVEVPN TTWTDIGGLE
SVKKELQELV QYPVEHPDKF LKFGMQPSRG VLFYGPPGCG KTLLAKAIAN ECQANFISVK
GPELLTMWFG ESEANVRDIF DKARSAAPCV LFFDELDSIA KARGGNVGDA GGAADRVINQ
ILTEMDGMGA KKNVFIIGAT NRPDIIDPAI LRPGRLDQLI YIPLPDDKSR EAILKANLRK
SPLAKEVDLT YIAKVTQGFS GADLTEICQR ACKLAIRQAI EAEIRREKER AENQNSAMDM
DEDDPVPEIT SAHFEEAMKF ARRSVSDNDI RKYEMFAQTL QQSRGFGQNF RFPGQTGNTS
GSGNNLPVNS PGDNGDDDLY S


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30-306 UBXD2 is an integral membrane protein of the endoplasmic reticulum (ER) that binds valosin-containing protein and promotes ER-associated protein degradation. 0.1 mg
EIAAB13274 C12orf8,Endoplasmic reticulum resident protein 28,Endoplasmic reticulum resident protein 29,Endoplasmic reticulum resident protein 31,ERp28,ERP28,ERp29,ERP29,ERp31,Homo sapiens,Human


 

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