SYVN1_MOUSE
ID SYVN1_MOUSE Reviewed; 612 AA.
AC Q9DBY1; Q80T88; Q8CGB5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=E3 ubiquitin-protein ligase synoviolin;
DE EC=2.3.2.27 {ECO:0000269|PubMed:29907570, ECO:0000269|PubMed:30389664};
DE AltName: Full=RING-type E3 ubiquitin transferase synoviolin {ECO:0000305};
DE AltName: Full=Synovial apoptosis inhibitor 1;
GN Name=Syvn1; Synonyms=Hrd1, Kiaa1810;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12975321; DOI=10.1101/gad.1096603;
RA Amano T., Yamasaki S., Yagishita N., Tsuchimochi K., Shin H., Kawahara K.,
RA Aratani S., Fujita H., Zhang L., Ikeda R., Fujii R., Miura N., Komiya S.,
RA Nishioka K., Maruyama I., Fukamizu A., Nakajima T.;
RT "Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for
RT arthropathy.";
RL Genes Dev. 17:2436-2449(2003).
RN [5]
RP INDUCTION BY ISCHEMIA.
RX PubMed=15519674; DOI=10.1016/j.molbrainres.2004.07.013;
RA Qi X., Okuma Y., Hosoi T., Kaneko M., Nomura Y.;
RT "Induction of murine HRD1 in experimental cerebral ischemia.";
RL Brain Res. Mol. Brain Res. 130:30-38(2004).
RN [6]
RP FUNCTION.
RX PubMed=15611074; DOI=10.1074/jbc.m410863200;
RA Yagishita N., Ohneda K., Amano T., Yamasaki S., Sugiura A., Tsuchimochi K.,
RA Shin H., Kawahara K., Ohneda O., Ohta T., Tanaka S., Yamamoto M.,
RA Maruyama I., Nishioka K., Fukamizu A., Nakajima T.;
RT "Essential role of synoviolin in embryogenesis.";
RL J. Biol. Chem. 280:7909-7916(2005).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17059562; DOI=10.1111/j.1471-4159.2006.04155.x;
RA Omura T., Kaneko M., Okuma Y., Orba Y., Nagashima K., Takahashi R.,
RA Fujitani N., Matsumura S., Hata A., Kubota K., Murahashi K., Uehara T.,
RA Nomura Y.;
RT "A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a
RT substrate of Parkin.";
RL J. Neurochem. 99:1456-1469(2006).
RN [8]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=17170702; DOI=10.1038/sj.emboj.7601490;
RA Yamasaki S., Yagishita N., Sasaki T., Nakazawa M., Kato Y., Yamadera T.,
RA Bae E., Toriyama S., Ikeda R., Zhang L., Fujitani K., Yoo E.,
RA Tsuchimochi K., Ohta T., Araya N., Fujita H., Aratani S., Eguchi K.,
RA Komiya S., Maruyama I., Higashi N., Sato M., Senoo H., Ochi T.,
RA Yokoyama S., Amano T., Kim J., Gay S., Fukamizu A., Nishioka K., Tanaka K.,
RA Nakajima T.;
RT "Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident
RT ubiquitin ligase 'Synoviolin'.";
RL EMBO J. 26:113-122(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, 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 [10]
RP INTERACTION WITH SEL1L.
RX PubMed=27064360; DOI=10.1038/srep20261;
RA Jeong H., Sim H.J., Song E.K., Lee H., Ha S.C., Jun Y., Park T.J., Lee C.;
RT "Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD
RT pathway.";
RL Sci. Rep. 6:20261-20261(2016).
RN [11]
RP FUNCTION, AND INTERACTION WITH NFE2L1.
RX PubMed=21911472; DOI=10.1128/mcb.05663-11;
RA Tsuchiya Y., Morita T., Kim M., Iemura S., Natsume T., Yamamoto M.,
RA Kobayashi A.;
RT "Dual regulation of the transcriptional activity of Nrf1 by beta-TrCP- and
RT Hrd1-dependent degradation mechanisms.";
RL Mol. Cell. Biol. 31:4500-4512(2011).
RN [12]
RP TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH CREB3L3, AND CATALYTIC
RP ACTIVITY.
RX PubMed=30389664; DOI=10.15252/embj.201898942;
RA Wei J., Chen L., Li F., Yuan Y., Wang Y., Xia W., Zhang Y., Xu Y., Yang Z.,
RA Gao B., Jin C., Melo-Cardenas J., Green R.M., Pan H., Wang J., He F.,
RA Zhang K., Fang D.;
RT "HRD1-ERAD controls production of the hepatokine FGF21 through CREBH
RT polyubiquitination.";
RL EMBO J. 37:0-0(2018).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IGLL1 AND VPREB1, AND
RP CATALYTIC ACTIVITY.
RX PubMed=29907570; DOI=10.1074/jbc.ra117.001267;
RA Yang Y., Kong S., Zhang Y., Melo-Cardenas J., Gao B., Zhang Y., Zhang D.D.,
RA Zhang B., Song J., Thorp E., Zhang K., Zhang J., Fang D.;
RT "The endoplasmic reticulum-resident E3 ubiquitin ligase Hrd1 controls a
RT critical checkpoint in B cell development in mice.";
RL J. Biol. Chem. 293:12934-12944(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin
CC specifically from endoplasmic reticulum-associated UBC7 E2 ligase and
CC transfers it to substrates, promoting their degradation
CC (PubMed:12975321, PubMed:15611074). Component of the endoplasmic
CC reticulum quality control (ERQC) system also called ER-associated
CC degradation (ERAD) involved in ubiquitin-dependent degradation of
CC misfolded endoplasmic reticulum proteins (PubMed:12975321,
CC PubMed:15611074). Also promotes the degradation of normal but naturally
CC short-lived proteins such as SGK. Protects cells from ER stress-induced
CC apoptosis. Sequesters p53/TP53 in the cytoplasm and promotes its
CC degradation, thereby negatively regulating its biological function in
CC transcription, cell cycle regulation and apoptosis (PubMed:17170702).
CC Required for embryogenesis (PubMed:15611074). Mediates the
CC ubiquitination and subsequent degradation of cytoplasmic NFE2L1
CC (PubMed:21911472). During the early stage of B cell development,
CC required for degradation of the pre-B cell receptor (pre-BCR) complex,
CC hence supporting further differentiation into mature B cells
CC (PubMed:29907570). {ECO:0000269|PubMed:12975321,
CC ECO:0000269|PubMed:15611074, ECO:0000269|PubMed:17170702,
CC ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:29907570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:29907570,
CC ECO:0000269|PubMed:30389664};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with p53/TP53
CC (PubMed:17170702). Interacts with HTT (By similarity). Component of the
CC HRD1 complex, which comprises at least SYNV1/HRD1, DERL1/2, FAM8A1,
CC HERPUD1/HERP, OS9, SEL1L and UBE2J1 (PubMed:27064360) (By similarity).
CC FAM8A1 is stabilized by interaction with SYNV1, which prevents its
CC proteasomal degradation. OS9 and UBE2J1 recruitment to the complex may
CC be mediated by SEL1L (By similarity). SYNV1 assembles with SEL1L and
CC FAM8A1 through its transmembrane domains, but interaction with its
CC cytoplasmic domain is required to confer stability to FAM8A1 and
CC enhance recruitment of HERPUD1 (By similarity). The HRD1 complex also
CC associates with VIMP and may transfer misfolded proteins from the
CC endoplasmic reticulum to VCP (By similarity). May form a complex with
CC ERLEC1; HSPA5; OS9 AND SEL1L (By similarity). Interacts with VCP (By
CC similarity). Interacts with UBXN6 (By similarity). Interacts with BAG6
CC (By similarity). Interacts with NFE2L1 (PubMed:21911472). Interacts
CC (via N-terminus) with components of the pre-B cell receptor, including
CC IGLL1 and VPREB1 (PubMed:29907570). Interacts with CREB3L3; this
CC interaction leads to CREB3L3 ubiquitination and proteasomal degradation
CC (PubMed:30389664). {ECO:0000250|UniProtKB:Q86TM6,
CC ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:21911472,
CC ECO:0000269|PubMed:27064360, ECO:0000269|PubMed:29907570,
CC ECO:0000269|PubMed:30389664}.
CC -!- INTERACTION:
CC Q9DBY1; P57716: Ncstn; NbExp=2; IntAct=EBI-644384, EBI-998934;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:29907570}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:17059562}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBY1-2; Sequence=VSP_023779, VSP_023780, VSP_023781,
CC VSP_023782, VSP_023783;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in bone,
CC spleen, lung and testis. In the brain, present in neurons but not in
CC glial cells. Up-regulated in synovial tissues from mice with collagen-
CC induced arthritis (at protein level). Expressed in the liver
CC (PubMed:30389664). {ECO:0000269|PubMed:12975321,
CC ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:30389664}.
CC -!- INDUCTION: Up-regulated in conditions of cerebral ischemia
CC (PubMed:15519674). In the liver, induced in postprandial conditions
CC (PubMed:30389664). {ECO:0000269|PubMed:15519674,
CC ECO:0000269|PubMed:30389664}.
CC -!- DOMAIN: The RING-type zinc finger is required for E3 ligase activity.
CC {ECO:0000250}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Mice overexpressing Syvn1 develop severe spontaneous
CC arthropathy. Mice lacking Syvn1 die in utero around 13.5 dpc due to
CC augmented apoptotic cell death.
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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DR EMBL; AK122558; BAC65840.3; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK004688; BAB23474.2; -; mRNA.
DR EMBL; BC042199; AAH42199.1; -; mRNA.
DR EMBL; BC046829; AAH46829.1; -; mRNA.
DR EMBL; BC057917; AAH57917.1; -; mRNA.
DR EMBL; BC080722; AAH80722.1; -; mRNA.
DR CCDS; CCDS29487.1; -. [Q9DBY1-1]
DR RefSeq; NP_001158181.1; NM_001164709.1.
DR RefSeq; NP_083045.4; NM_028769.5.
DR RefSeq; XP_006531913.1; XM_006531850.3.
DR AlphaFoldDB; Q9DBY1; -.
DR SMR; Q9DBY1; -.
DR BioGRID; 216511; 19.
DR IntAct; Q9DBY1; 4.
DR MINT; Q9DBY1; -.
DR STRING; 10090.ENSMUSP00000114843; -.
DR iPTMnet; Q9DBY1; -.
DR PhosphoSitePlus; Q9DBY1; -.
DR MaxQB; Q9DBY1; -.
DR PaxDb; Q9DBY1; -.
DR PeptideAtlas; Q9DBY1; -.
DR PRIDE; Q9DBY1; -.
DR ProteomicsDB; 254510; -. [Q9DBY1-1]
DR ProteomicsDB; 254511; -. [Q9DBY1-2]
DR DNASU; 74126; -.
DR GeneID; 74126; -.
DR KEGG; mmu:74126; -.
DR UCSC; uc008ggm.2; mouse. [Q9DBY1-1]
DR CTD; 84447; -.
DR MGI; MGI:1921376; Syvn1.
DR eggNOG; KOG0802; Eukaryota.
DR InParanoid; Q9DBY1; -.
DR OrthoDB; 897451at2759; -.
DR PhylomeDB; Q9DBY1; -.
DR TreeFam; TF318635; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 74126; 18 hits in 74 CRISPR screens.
DR ChiTaRS; Syvn1; mouse.
DR PRO; PR:Q9DBY1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9DBY1; protein.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:UniProtKB.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0036503; P:ERAD pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0002327; P:immature B cell differentiation; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0006986; P:response to unfolded protein; ISO:MGI.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032832; E3_lig_synoviolin/Hrd1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763:SF169; PTHR22763:SF169; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Endoplasmic reticulum;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..612
FT /note="E3 ubiquitin-protein ligase synoviolin"
FT /id="PRO_0000280549"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..41
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..140
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..224
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 291..330
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..251
FT /note="Involved in FAM8A1 interaction"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT REGION 21..42
FT /note="Interaction with SEL1L"
FT /evidence="ECO:0000269|PubMed:27064360"
FT REGION 236..270
FT /note="Interaction with p53/TP53"
FT /evidence="ECO:0000269|PubMed:17170702"
FT REGION 337..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..529
FT /note="HAF-H domain; necessary to form higher-order Hrd1
FT complexes"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT REGION 530..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT VAR_SEQ 75
FT /note="E -> EVICWWPQRTGFRGGYPNDWFSYHPLLTPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023779"
FT VAR_SEQ 127..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023780"
FT VAR_SEQ 369..375
FT /note="FPQGLLP -> CKWPFIC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023781"
FT VAR_SEQ 577..578
FT /note="AP -> GK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023782"
FT VAR_SEQ 579..612
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023783"
FT CONFLICT 287
FT /note="V -> M (in Ref. 2; BAB23474 and 3; AAH46829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 67296 MW; 8F7620E5016DF1F2 CRC64;
MFRTAVMMAA SLALTGAVVA HAYYLKHQFY PTVVYLTKSS PSMAVLYIQA FVLVFLLGKV
MGKVFFGQLR AAEMEHLLER SWYAVTETCL AFTVFRDDFS PRFVALFTLL LFLKCFHWLA
EDRVDFMERS PNISWLFHCR IVSLMFLLGI LDFLFVSHAY HSILTRGASV QLVFGFEYAI
LMTMVLTIFI KYVLHSVDLQ SENPWDNKAV YMLYTELFTG FIKVLLYMAF MTIMIKVHTF
PLFAIRPMYL AMRQFKKAVT DAIMSRRAIR NMNTLYPDAT PEELQAVDNV CIICREEMVT
GAKRLPCNHI FHTSCLRSWF QRQQTCPTCR MDVLRASLPA QSPPPPEPAD QGPPPAPHPQ
PLLPQPPNFP QGLLPPFPPG MFPLWPPMGP FPPVPPPPSS GEAAAPPPTS TAVSRPSGAA
TTTAAGTSTS APAPGSVPGP EAGPAPGFPF PPPWMGMPLP PPFAFPPMPV PPAGFAGLTP
EELRALEGHE RQHLEARLQS LRNIHTLLDA AMLQINQYLT VLASLGPPRP ATSVNPTEET
ASTVVSAAPS TSAPSSEAPT PSPGASPPIP EAEKPPAPES VGIVEELPED GEPDAAELRR
RRLQKLESPV AH
