位置:首页 > 蛋白库 > MINA1_CAEEL
MINA1_CAEEL
ID   MINA1_CAEEL             Reviewed;         393 AA.
AC   Q93367;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Messenger RNA-binding inhibitor of apoptosis 1 {ECO:0000303|PubMed:30728462};
GN   Name=mina-1 {ECO:0000303|PubMed:30728462};
GN   ORFNames=C41G7.3 {ECO:0000312|WormBase:C41G7.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0007744|PDB:6FBL}
RP   STRUCTURE BY NMR OF 254-334, FUNCTION, INTERACTION WITH WAGO-4, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP   OF 276-ASN-ARG-277.
RX   PubMed=30728462; DOI=10.1038/s41418-019-0291-z;
RA   Sendoel A., Subasic D., Ducoli L., Keller M., Michel E., Kohler I.,
RA   Singh K.D., Zheng X., Bruemmer A., Imig J., Kishore S., Wu Y., Kanitz A.,
RA   Kaech A., Mittal N., Matia-Gonzalez A.M., Gerber A.P., Zavolan M.,
RA   Aebersold R., Hall J., Allain F.H., Hengartner M.O.;
RT   "MINA-1 and WAGO-4 are part of regulatory network coordinating germ cell
RT   death and RNAi in C. elegans.";
RL   Cell Death Differ. 26:2157-2178(2019).
CC   -!- FUNCTION: RNA-binding protein which binds to its own mRNA and target
CC       mRNAs to negatively regulate gene expression to modulate apoptosis and
CC       differentiation in the germline (PubMed:30728462). Negatively regulates
CC       the expression of the argonaute protein wago-4, and may thus play a
CC       role in RNA-mediated gene silencing (RNAi) in the germline
CC       (PubMed:30728462). {ECO:0000269|PubMed:30728462}.
CC   -!- SUBUNIT: May interact with wago-4. {ECO:0000269|PubMed:30728462}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:30728462}.
CC   -!- TISSUE SPECIFICITY: Expressed throughout the germline and in oocytes
CC       (at protein level). {ECO:0000269|PubMed:30728462}.
CC   -!- DOMAIN: The KH-like 3 domain is required for binding to RNA.
CC       {ECO:0000269|PubMed:30728462}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC       apoptosis and increased sensitivity to DNA damage-induced apoptosis in
CC       response to ionizing radiation in the germline.
CC       {ECO:0000269|PubMed:30728462}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX284601; CAB02840.2; -; Genomic_DNA.
DR   RefSeq; NP_492528.2; NM_060127.5.
DR   PDB; 6FBL; NMR; -; A=254-334.
DR   PDBsum; 6FBL; -.
DR   AlphaFoldDB; Q93367; -.
DR   BMRB; Q93367; -.
DR   SMR; Q93367; -.
DR   STRING; 6239.C41G7.3; -.
DR   EPD; Q93367; -.
DR   PaxDb; Q93367; -.
DR   EnsemblMetazoa; C41G7.3.1; C41G7.3.1; WBGene00008061.
DR   GeneID; 172786; -.
DR   KEGG; cel:CELE_C41G7.3; -.
DR   UCSC; C41G7.3; c. elegans.
DR   CTD; 172786; -.
DR   WormBase; C41G7.3; CE42810; WBGene00008061; mina-1.
DR   eggNOG; ENOG502TG75; Eukaryota.
DR   HOGENOM; CLU_700640_0_0_1; -.
DR   InParanoid; Q93367; -.
DR   OMA; ITVHTEV; -.
DR   OrthoDB; 1096930at2759; -.
DR   PRO; PR:Q93367; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00008061; Expressed in germ line (C elegans) and 3 other tissues.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   Pfam; PF00013; KH_1; 1.
DR   SMART; SM00322; KH; 2.
DR   SUPFAM; SSF54791; SSF54791; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; RNA-binding.
FT   CHAIN           1..393
FT                   /note="Messenger RNA-binding inhibitor of apoptosis 1"
FT                   /id="PRO_0000448350"
FT   REGION          12..76
FT                   /note="KH 1-like"
FT                   /evidence="ECO:0000305|PubMed:30728462"
FT   REGION          79..157
FT                   /note="KH 2-like"
FT                   /evidence="ECO:0000305|PubMed:30728462"
FT   REGION          259..322
FT                   /note="KH 3-like"
FT                   /evidence="ECO:0000269|PubMed:30728462,
FT                   ECO:0007744|PDB:6FBL"
FT   REGION          328..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         276..277
FT                   /note="NR->DD: Impairs RNA-binding."
FT                   /evidence="ECO:0000269|PubMed:30728462"
FT   STRAND          259..265
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   HELIX           267..270
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   HELIX           271..274
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   HELIX           279..288
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   STRAND          305..313
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   HELIX           314..321
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   TURN            322..330
FT                   /evidence="ECO:0007829|PDB:6FBL"
FT   HELIX           331..333
FT                   /evidence="ECO:0007829|PDB:6FBL"
SQ   SEQUENCE   393 AA;  43736 MW;  792E48CE9E952DDD CRC64;
     MDDSTPYPVP QELYIPQKMK AFMAEPQGCA LVAALEGQFQ CSIVVINDHL SVISSADGVA
     VDINQIEKIL RDVWRKRDVQ IMIREAALNA SCTHICHTLL PRAYCAVVLF FSSDLQRRSR
     CTDIIIDQFT GKVTMFGTEQ AVNKAREMMI ECLTEHFGLL EMNIPPTQRT TRMGYTNSYN
     PEIRTHLPPN SFLNSVFPMG EPNAILTSTP PTTSIMDEPL LSASLEKHLL FPSDFSVPPP
     RLSPVQELPL TPPKTCVVEK IKQWIPTTEV GKILGNRAAV KKHIERQFNC VITVHTEVQS
     SFGATPVEIV AQNKEQCQEA RNAVMSLMQS HQDKPASNPP DSGFSTPGSP FTSDSSSTTP
     EKRGNSRQYH RGSFRDQPKV MLALTPRKLS PSD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024