NEUL2_MOUSE
ID NEUL2_MOUSE Reviewed; 285 AA.
AC Q9D0S4;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Neuralized-like protein 2;
GN Name=Neurl2; Synonyms=Ozz;
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=Embryo;
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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP CTNNB1, AND RECONSTITUTION OF AN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX.
RX PubMed=14960280; DOI=10.1016/s1534-5807(04)00020-6;
RA Nastasi T., Bongiovanni A., Campos Y., Mann L., Toy J.N., Bostrom J.,
RA Rottier R., Hahn C., Conaway J.W., Harris A.J., D'Azzo A.;
RT "Ozz-E3, a muscle-specific ubiquitin ligase, regulates beta-catenin
RT degradation during myogenesis.";
RL Dev. Cell 6:269-282(2004).
CC -!- FUNCTION: Plays an important role in the process of myofiber
CC differentiation and maturation. Probable substrate-recognition
CC component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3
CC ubiquitin-protein ligase complex, which mediates the ubiquitination of
CC proteins. Probably contributes to catalysis through recognition and
CC positioning of the substrate and the ubiquitin-conjugating enzyme.
CC During myogenesis, controls the ubiquitination and degradation of the
CC specific pool of CTNNB1/beta-catenin located at the sarcolemma.
CC {ECO:0000269|PubMed:14960280}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Probable component the ECS(NEURL2) E3 ubiquitin-protein ligase
CC complex consisting of ELOB/Elongin B, ELOC/Elongin C, CUL5, RBX1 and
CC NEURL2. Interacts with CTNNB1. {ECO:0000269|PubMed:14960280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14960280}. Note=In
CC primary myoblasts, localized predominantly at the tips of
CC differentiating myofibers.
CC -!- TISSUE SPECIFICITY: Expressed specifically in skeletal and cardiac
CC muscles. {ECO:0000269|PubMed:14960280}.
CC -!- DEVELOPMENTAL STAGE: At 10 dpc, confined to the developing heart and
CC the somites at the tips of the myotomal cells near the intermyotomal
CC septum. At 14 to 15 dpc, accumulates near the myotendinous junctions,
CC the site of sarcomere assembly in growing myotubes. Present in
CC negligible amounts in proliferating myoblasts, induced during
CC differentiation.
CC -!- DOMAIN: The SOCS domain mediates the interaction with ELOB and ELOC,
CC while the NHR domain may be involved in ubiquitination substrate
CC binding. {ECO:0000250}.
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DR EMBL; AK004524; BAB23346.1; -; mRNA.
DR CCDS; CCDS38330.1; -.
DR AlphaFoldDB; Q9D0S4; -.
DR SMR; Q9D0S4; -.
DR CORUM; Q9D0S4; -.
DR STRING; 10090.ENSMUSP00000041806; -.
DR PaxDb; Q9D0S4; -.
DR PRIDE; Q9D0S4; -.
DR ProteomicsDB; 252825; -.
DR MGI; MGI:3043305; Neurl2.
DR eggNOG; KOG4625; Eukaryota.
DR InParanoid; Q9D0S4; -.
DR PhylomeDB; Q9D0S4; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR ChiTaRS; Jag1; mouse.
DR PRO; PR:Q9D0S4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D0S4; protein.
DR GO; GO:0005927; C:muscle tendon junction; IDA:MGI.
DR GO; GO:0030891; C:VCB complex; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0030239; P:myofibril assembly; IMP:MGI.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR037962; Neuralized.
DR InterPro; IPR006573; NHR_dom.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR12429; PTHR12429; 1.
DR Pfam; PF07177; Neuralized; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00588; NEUZ; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR PROSITE; PS51065; NHR; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..285
FT /note="Neuralized-like protein 2"
FT /id="PRO_0000181258"
FT DOMAIN 23..244
FT /note="NHR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT DOMAIN 250..285
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 31537 MW; 4A0B7CFEF27B10B8 CRC64;
MADPSEHVGL GGPRSPARPE PPPTRFHQVH GANIRMDPSG TRATRVESFA HGVCFSREPL
APGQVFLVEI EEKELGWCGH LRLGLTALDP ASLAAVPEFS LPDLVSLGHS WVFAITRHHN
RVPREGQPEA EAAVPSGPQA LLVEPYLRIE QFRIPRDRLV GRSRPGLYSH LLDQLYEQNV
LPPTARRSRL GVLFCPREDG TADMHIIING EDMGPSARGL PAAQPLYAVV DVFASTKSVR
LVQLEYGLPS LQTLCRLVIH KRVVHRLAID VLHLPKGLKD FCKYE
