MBNL2_RAT
ID MBNL2_RAT Reviewed; 373 AA.
AC F2Z3T4;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Muscleblind-like protein 2;
GN Name=Mbnl2;
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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19457059; DOI=10.1111/j.1471-4159.2009.06184.x;
RA Kim J.S., Coon S.L., Weller J.L., Blackshaw S., Rath M.F., Moller M.,
RA Klein D.C.;
RT "Muscleblind-like 2: circadian expression in the mammalian pineal gland is
RT controlled by an adrenergic-cAMP mechanism.";
RL J. Neurochem. 110:756-764(2009).
CC -!- FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts
CC either as activator or repressor of splicing on specific pre-mRNA
CC targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion
CC but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle.
CC Antagonizes the alternative splicing activity pattern of CELF proteins.
CC RNA-binding protein that binds to 5'ACACCC-3' core sequence, termed
CC zipcode, within the 3'UTR of ITGA3. Binds to CUG triplet repeat
CC expansion in myotonic dystrophy muscle cells by sequestering the target
CC RNAs. Seems to regulate expression and localization of ITGA3 by
CC transporting it from the nucleus to cytoplasm at adhesion plaques. May
CC play a role in myotonic dystrophy pathophysiology (DM) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ITGA3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VZF2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5VZF2}. Note=Greater concentration in the
CC nucleus. Expressed in or near large cytoplasmic adhesion plaques.
CC Location in the cytoplasm is microtubule-dependent.
CC {ECO:0000250|UniProtKB:Q5VZF2}.
CC -!- TISSUE SPECIFICITY: Expressed in the cerebellum, pineal gland and
CC skeletal muscle. In the pineal gland, expressed in pinealocytes, not in
CC perivascular spaces (at protein level). {ECO:0000269|PubMed:19457059}.
CC -!- INDUCTION: Exhibits night/day variations with a 9-fold increased
CC expression at night in the pineal gland (at protein level). A light
CC pulse of 1 hour is sufficient to decrease mRNA levels. Up-regulation is
CC due to a large degree to the release of norepinephrine from nerve
CC terminals in the pineal gland and cAMP signaling pathway.
CC {ECO:0000269|PubMed:19457059}.
CC -!- SIMILARITY: Belongs to the muscleblind family. {ECO:0000305}.
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DR RefSeq; NP_001104534.1; NM_001111064.1.
DR AlphaFoldDB; F2Z3T4; -.
DR SMR; F2Z3T4; -.
DR STRING; 10116.ENSRNOP00000014300; -.
DR iPTMnet; F2Z3T4; -.
DR PhosphoSitePlus; F2Z3T4; -.
DR jPOST; F2Z3T4; -.
DR PaxDb; F2Z3T4; -.
DR Ensembl; ENSRNOT00000014300; ENSRNOP00000014300; ENSRNOG00000010737.
DR GeneID; 680445; -.
DR KEGG; rno:680445; -.
DR CTD; 10150; -.
DR RGD; 1591755; Mbnl2.
DR eggNOG; KOG2494; Eukaryota.
DR GeneTree; ENSGT00950000182897; -.
DR HOGENOM; CLU_053536_0_0_1; -.
DR InParanoid; F2Z3T4; -.
DR OMA; PTXNSEI; -.
DR OrthoDB; 1543798at2759; -.
DR PRO; PR:F2Z3T4; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000010737; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; F2Z3T4; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 4.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..373
FT /note="Muscleblind-like protein 2"
FT /id="PRO_0000414482"
FT ZN_FING 13..41
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 47..73
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 176..204
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 212..238
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 373 AA; 40156 MW; 22F5B46101976FA5 CRC64;
MALNVAPVRD TKWLTLEVCR QYQRGTCSRS DEECKFAHPP KSCQVENGRV IACFDSLKGR
CSRENCKYLH PPTHLKTQLE INGRNNLIQQ KTAAAMLAQQ MQFMFPGTPL HPVPTFPVGP
TIGTNAAISF APYLAPVTPG VGLVPTEVLP TTPVIVPGSP PVTVPGSTAT QKLLRTDKLE
VCREFQRGNC ARGETDCRFA HPADSTMIDT NDNTVTVCMD YIKGRCMREK CKYFHPPAHL
QAKIKAAQHQ ANQAAVAAQA AAAAATVMTQ STAKALKRPL EATVDLAFPP GALHPLPKRQ
ALEKSNGAST VFNPSVLHYQ QALTSAQLQQ HTAFIPTVPM MHSATSATVS AATTPATSVP
FAATATANQI ILK
