ZSWM2_MOUSE
ID ZSWM2_MOUSE Reviewed; 631 AA.
AC Q9D9X6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=E3 ubiquitin-protein ligase Zswim2;
DE EC=2.3.2.27;
DE AltName: Full=MEKK1-related protein X;
DE Short=MEX;
DE AltName: Full=RING-type E3 ubiquitin transferase Zswim2;
DE AltName: Full=ZZ-type zinc finger-containing protein 2;
DE AltName: Full=Zinc finger SWIM domain-containing protein 2;
GN Name=Zswim2;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP TISSUE SPECIFICITY, FUNCTION, UBIQUITINATION, SUBUNIT, DOMAIN, INTERACTION
RP WITH UBE2D1, AND MUTAGENESIS OF CYS-66 AND CYS-168.
RX PubMed=16522193; DOI=10.1042/bj20051814;
RA Nishito Y., Hasegawa M., Inohara N., Nunez G.;
RT "MEX is a testis-specific E3 ubiquitin ligase that promotes death receptor-
RT induced apoptosis.";
RL Biochem. J. 396:411-417(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction with
CC the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating enzymes.
CC {ECO:0000269|PubMed:16522193}.
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;
CC -!- SUBUNIT: Dimer. Interacts with UBE2D1. {ECO:0000269|PubMed:16522193}.
CC -!- TISSUE SPECIFICITY: Expressed only in testis.
CC {ECO:0000269|PubMed:16522193}.
CC -!- DOMAIN: The SWIM-type zinc finger is required for ubiquitination
CC activity. {ECO:0000269|PubMed:16522193}.
CC -!- PTM: Polyubiquitinated. Polyubiquitination is followed by degradation
CC via the proteasome. {ECO:0000269|PubMed:16522193}.
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DR EMBL; AK006367; BAB24549.1; -; mRNA.
DR CCDS; CCDS16183.1; -.
DR RefSeq; NP_082240.1; NM_027964.2.
DR AlphaFoldDB; Q9D9X6; -.
DR SMR; Q9D9X6; -.
DR BioGRID; 214986; 4.
DR STRING; 10090.ENSMUSP00000044913; -.
DR iPTMnet; Q9D9X6; -.
DR PhosphoSitePlus; Q9D9X6; -.
DR PaxDb; Q9D9X6; -.
DR PRIDE; Q9D9X6; -.
DR ProteomicsDB; 302154; -.
DR Antibodypedia; 34014; 101 antibodies from 18 providers.
DR DNASU; 71861; -.
DR Ensembl; ENSMUST00000038223; ENSMUSP00000044913; ENSMUSG00000034552.
DR GeneID; 71861; -.
DR KEGG; mmu:71861; -.
DR UCSC; uc008kif.1; mouse.
DR CTD; 151112; -.
DR MGI; MGI:1919111; Zswim2.
DR VEuPathDB; HostDB:ENSMUSG00000034552; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00390000006826; -.
DR HOGENOM; CLU_029121_0_0_1; -.
DR InParanoid; Q9D9X6; -.
DR OMA; KISQHFP; -.
DR OrthoDB; 797346at2759; -.
DR PhylomeDB; Q9D9X6; -.
DR TreeFam; TF333237; -.
DR BioGRID-ORCS; 71861; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9D9X6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D9X6; protein.
DR Bgee; ENSMUSG00000034552; Expressed in spermatid and 33 other tissues.
DR ExpressionAtlas; Q9D9X6; baseline and differential.
DR Genevisible; Q9D9X6; MM.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR InterPro; IPR039903; Zswim2.
DR PANTHER; PTHR21540; PTHR21540; 1.
DR Pfam; PF04434; SWIM; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS50966; ZF_SWIM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..631
FT /note="E3 ubiquitin-protein ligase Zswim2"
FT /id="PRO_0000223098"
FT ZN_FING 54..87
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT ZN_FING 147..199
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 230..281
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 344..386
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 139..348
FT /note="UBE2D1-binding"
FT REGION 589..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MUTAGEN 66
FT /note="C->S: Abrogates ubiquitination activity and the
FT ability to promote DR4- and Fas-induced apoptosis."
FT /evidence="ECO:0000269|PubMed:16522193"
FT MUTAGEN 168
FT /note="C->S: Abrogates ubiquitination activity."
FT /evidence="ECO:0000269|PubMed:16522193"
SQ SEQUENCE 631 AA; 71793 MW; 4DBD3CCD323F8A8E CRC64;
MLRGGCKASE KRRHLSESLS WQQDQALSSS IYLLRQIGPT GFLLKEEEPE KGDFRVLLGN
PHECSCPTFL KRGELCKHIC WVLLKKFKLP RNHESAFQLG LTEGEINDLL RGIHQVQAPQ
LRASDETAQV EEDGYLKQKD INAGDICPIC QEVLLEKKLP VTFCRFGCGN NVHIKCMRIL
ANYQDTGSDS SVLRCPLCRE EFAPLKVILE EFKNSNKLIT ISEKERLDKH LGIPCNNCNQ
LPIEGRCYKC TECVEYHLCQ ECFDSCCHSS HAFASREKRN QRWRSVEKRS EVMKYLNTEN
EGEAKPGCFQ EKQGQFYTPK HVVKSLPLLM ITKKSKLLAP GYQCRLCLKS FSFGQYTRLL
PCTHKFHRKC IDNWLLHKCN SCPIDRQVIY NPLIWKGIAT DGQAHQLASS KDIACLSKQQ
EPKLFIPGTG LVLKGKRMGV LPSIPQYNSK VLTTLQNPSD NYQNITMDDL CSVKLDNSNS
RKLVFGYKIS KQFPTYLKNP TTGQTPSQTF LPSLPHKNII CLTGRESPHI YEKDHIGQSQ
KTSRGYEHIN YNTRKSLGSR LRQHKRSSAL SSEDLNLTIN LGTTKLSLSK RQNNSMGKVR
QKLGHPPRRP AYPPLQTQNA ALSLIMQGIQ L
