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Database: UniProt
Entry: I3JN14_ORENI
LinkDB: I3JN14_ORENI
Original site: I3JN14_ORENI 
ID   I3JN14_ORENI            Unreviewed;      1327 AA.
AC   I3JN14;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Clustered mitochondria protein homolog {ECO:0000256|HAMAP-Rule:MF_03013};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000010258.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000010258.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: mRNA-binding protein involved in proper cytoplasmic
CC       distribution of mitochondria. Specifically binds mRNAs of nuclear-
CC       encoded mitochondrial proteins in the cytoplasm and regulates transport
CC       or translation of these transcripts close to mitochondria, playing a
CC       role in mitochondrial biogenesis. {ECO:0000256|HAMAP-Rule:MF_03013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03013}.
CC       Cytoplasmic granule {ECO:0000256|HAMAP-Rule:MF_03013}.
CC   -!- SIMILARITY: Belongs to the CLU family. {ECO:0000256|HAMAP-
CC       Rule:MF_03013}.
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DR   STRING; 8128.ENSONIP00000010258; -.
DR   Ensembl; ENSONIT00000010267.2; ENSONIP00000010258.2; ENSONIG00000008146.2.
DR   eggNOG; KOG1839; Eukaryota.
DR   GeneTree; ENSGT00390000012485; -.
DR   HOGENOM; CLU_003256_1_0_1; -.
DR   InParanoid; I3JN14; -.
DR   OMA; HPVWDKD; -.
DR   TreeFam; TF300565; -.
DR   Proteomes; UP000005207; Linkage group LG14.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:UniProtKB-UniRule.
DR   CDD; cd15466; CLU-central; 1.
DR   Gene3D; 3.30.2280.10; Hypothetical protein (hspc210); 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   HAMAP; MF_03013; CLU; 1.
DR   InterPro; IPR033646; CLU-central.
DR   InterPro; IPR025697; CLU_dom.
DR   InterPro; IPR028275; CLU_N.
DR   InterPro; IPR027523; CLU_prot.
DR   InterPro; IPR023231; GSKIP_dom_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR12601:SF10; CLUSTERED MITOCHONDRIA PROTEIN HOMOLOG; 1.
DR   PANTHER; PTHR12601; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT EIF-3; 1.
DR   Pfam; PF13236; CLU; 1.
DR   Pfam; PF15044; CLU_N; 1.
DR   Pfam; PF12807; eIF3_p135; 2.
DR   Pfam; PF13424; TPR_12; 2.
DR   SUPFAM; SSF103107; Hypothetical protein c14orf129, hspc210; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS51823; CLU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013}.
FT   DOMAIN          342..584
FT                   /note="Clu"
FT                   /evidence="ECO:0000259|PROSITE:PS51823"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1303..1327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1327 AA;  148006 MW;  524D9EFC1D0EB8D8 CRC64;
     EECARHSADT AMVNGDGAHE HTEETDSKQD GNGEADGGEE SNEQEVIVIQ DTGFTVKIQA
     PGTEPFDLQV SPQEMVQEIH QVLMDREDTC HRTCFSLQLD GNVLDNFAEL KSIEGLQEGS
     VLKVVEEPYT VREARIHVRH IRDLLKSLDP SDAYNGVDCN SLSFLSIFTD GDLGETGKRK
     KKGNEMEQID CTPPEHILPG SKERPLVPLQ PQNKDWKPMQ CLKVLTMSGW NPPPGNRKMH
     GDLMYLYIVT VEERHVSVTA STRGFYLNQS TTYTFNPKPA NPSFLSHSLV ELLSQISPAF
     KKNFTALQKK RVQRHPFERI ATPFQVYSWT APQVDHAMDC VRAEDAYTSR LGYEEHIPGQ
     TRDWNEELQT TRELPRKNLP ERLLRERAIF KVHSDFAAAA TRGAMAVIDG NVMAINPGEE
     TRMQMFIWNN IFFSLGFDVR DHYRELGGDA AAHAAPTNDL NGVRAYSGVD VEGLYTLGTV
     VVDYRGYRVT AQSIIPGILE REQEQSVIYG SIDFGKTVVS HGKYLELLEK TSRPLKVQRH
     SVLNEKNDTV ELCSSVECKG IIGNDGRHYI LDLLRTFPPD LNFLPVDGVE LSPECQRLGF
     PAMTLLLFLM AALQLMQHKA NRDSNKTDTP AITETSETLT ESKASTTQTD TAQTTATDSS
     KATDISTDST SQTDNASTAA SQTGTDSEEN SSKPTTNGPV DPTATQNGEC KGPLEGKELE
     ESIPGLAQAK ELAETLVAED GSSIDPKSRE VVLNACKAVG SISDTAFDIR FNPDIFSPGV
     RFPEESADDI QKQKQLLKDA AAFLVSCQVP TLVKDCLDHS ALPMDGASLT EALHQRGINV
     RYLGTVLEFM EKTPAKAQLE LVTFNGTTFS LSALSAAVSH FLNCFLSSFP DAVAHLPPDE
     LVSRRKNRKR RNRVPGGGDN TAWASLTPSE LWKNIASEAQ SYYHFTLQCE SVDQVVEKFG
     LQKITLLREI SVKTGIQILI KEYNFDSRHK PAFTEEDILN IFPVVKHVNP KATDAFHFFQ
     SGQAKVQQGF LKEGCELINE ALNLFNNVYG AMHVEICSCL RLLARLNYIL GDHPEALSNQ
     QKAVLMSERV LGIEHPNTIQ EYMHLALYCF ANNQLSTALK LLYRARYLML LICGEDHPEM
     ALLDSNIGLV LHGVMEYDLS LRFLENALTI NTKYHGPRSL KVALSHHLVA RVYESKAEFR
     SALQHEKEGY TIYKNQMGEA HEKTKESSEY LKYLTQQAVA LQRTMNEIYK NGSNASIMPL
     KFTAPSMATI LDQLNIINGI IFIPLSPKDL ENLKAEVQRR QQLQELGKGE EPAEDRSLEL
     EDKIPID
//
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