PZRN3_RAT
ID PZRN3_RAT Reviewed; 1062 AA.
AC P68907;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase PDZRN3;
DE EC=2.3.2.27;
DE AltName: Full=PDZ domain-containing RING finger protein 3;
DE AltName: Full=RING-type E3 ubiquitin transferase PDZRN3 {ECO:0000305};
DE AltName: Full=Semaphorin cytoplasmic domain-associated protein 3;
DE Short=Protein SEMACAP3;
GN Name=Pdzrn3; Synonyms=Semcap3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP INTERACTION WITH NLGN1 AND EFNB2.
RX PubMed=15458844; DOI=10.1016/j.neuropharm.2004.06.023;
RA Meyer G., Varoqueaux F., Neeb A., Oschlies M., Brose N.;
RT "The complexity of PDZ domain-mediated interactions at glutamatergic
RT synapses: a case study on neuroligin.";
RL Neuropharmacology 47:724-733(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Plays an important role in
CC regulating the surface level of MUSK on myotubes. Mediates the
CC ubiquitination of MUSK, promoting its endocytosis and lysosomal
CC degradation. Might contribute to terminal myogenic differentiation.
CC {ECO:0000250|UniProtKB:Q69ZS0}.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with NLGN1 and EFNB2. Interacts with UBE2D2 and with
CC MUSK via the first PDZ domain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q69ZS0}. Cytoplasm
CC {ECO:0000250|UniProtKB:E7FDW2}. Note=Localizes to the postsynaptic
CC region of neuromuscular junctions. {ECO:0000250|UniProtKB:Q69ZS0}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
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DR EMBL; AABR03034730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03032044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03034150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03035737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03033172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03038940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P68907; -.
DR BMRB; P68907; -.
DR SMR; P68907; -.
DR IntAct; P68907; 1.
DR STRING; 10116.ENSRNOP00000037674; -.
DR iPTMnet; P68907; -.
DR PhosphoSitePlus; P68907; -.
DR PaxDb; P68907; -.
DR PRIDE; P68907; -.
DR UCSC; RGD:1305250; rat.
DR RGD; 1305250; Pdzrn3.
DR eggNOG; KOG0297; Eukaryota.
DR eggNOG; KOG0312; Eukaryota.
DR InParanoid; P68907; -.
DR PhylomeDB; P68907; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P68907; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR001293; Znf_TRAF.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1062
FT /note="E3 ubiquitin-protein ligase PDZRN3"
FT /id="PRO_0000055919"
FT DOMAIN 248..338
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 418..502
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ZN_FING 18..56
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 100..158
FT /note="TRAF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT REGION 544..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 679..704
FT /evidence="ECO:0000255"
FT COILED 812..1062
FT /evidence="ECO:0000255"
FT COMPBIAS 567..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZS0"
SQ SEQUENCE 1062 AA; 119289 MW; 9EB3D2115C864037 CRC64;
MGFELDRFDG EVDPDLKCAL CHKVLEDPLT TPCGHVFCAG CVLPWVVQEG SCPSRCRGRL
SAKELNHVLP LKRLILKLDI KCAHAARGCG RVVKLQDLPE HLERCDFAPA RCRHAGCGQL
LLRRDVEAHM RDACDARPVG RCQEGCGLPL THGEQRAGGH CCARALRAHN GALQARLGAL
HKALKKEALR AGKREKSLLA QLAAAQLELQ MTALRYQKKF TEYSARLDSL SRCVAAPPGG
GEETKSLTLV LHRDSGSLGF NIIGGRPCVD NQDGSSSEGI FVSKIVDSGP AAKEGGLQIH
DRIIEVNGKD LSRATHDQAV EAFKTAKEPI VVQVLRRTPR TKMFTPASES QLVDTGTQTD
ITFEHIMALT KISSPSPPVL GPYLLPEEHP SSHEYYDPND YMGDIHQDMD REELELEEVG
LYRMNSQDKL GLTVCYRTDD EDDIGIYISE IDPNSIAAKD GRIREGDRII QINGIEVQNR
EEAVALLTSE ENKNFSLLIA RPELQLDEGW MDDDRNDFLD DLHMDMLEEQ HHQAMQFTAS
VLQQKKHEED GGTTDTATIL SNQHEKDSGV GRTDESTRND ESSEQENNGE DATASSNPLA
GQRKLTCSQD TLGSGDLPFS NESFISADCT DVDYLGIPED ECERFRELLE LKCQVQSTSP
YSLYYPSSPL DAAGKGDPES VDKELELLNE ELRSIELECL SIVRAHKMQQ LKEQYRESWM
LHHSGFRNYN TSVDVRRHEL SDITELPEKS DKDSSSAYNT GESCRSTPLT LEISPDNSLR
RVAEGSSEGA TANMEAYRPS PKNLLAITED PEVSTPNYNP GAKELDPSQA LEIKERRVSD
GSRSPTASPK LGSAYLPSYH HSPYKHAHIP AHAQHYQSYM HLIQQKSAVE YAQSQMSLVS
MCKDLNSSNS AEPRMEWKVK IRSDGTRYIT KRPVRDRLLR ERALKIREER SGLTTDDDAM
SEMKMGRYWS KEERKQHLVK AKEQRRRREF MMQSRLDCLK EQQASDDRKE MNILELSHKK
MMKKRNKKIF DNWMTIQELL THGTKSPDGT RVYNSFLSVT TV
