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Database: UniProt
Entry: A0A1U8BIW9_MESAU
LinkDB: A0A1U8BIW9_MESAU
Original site: A0A1U8BIW9_MESAU 
ID   A0A1U8BIW9_MESAU        Unreviewed;      1348 AA.
AC   A0A1U8BIW9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Clustered mitochondria protein homolog {ECO:0000256|HAMAP-Rule:MF_03013};
GN   Name=Cluh {ECO:0000313|RefSeq:XP_012967172.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012967172.1};
RN   [1] {ECO:0000313|RefSeq:XP_012967172.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_012967172.1; XM_013111718.2.
DR   GeneID; 101843293; -.
DR   CTD; 23277; -.
DR   OrthoDB; 927222at2759; -.
DR   Proteomes; UP000189706; Unplaced.
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:SF6; 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; 1.
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:UP000189706};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013}.
FT   DOMAIN          373..615
FT                   /note="Clu"
FT                   /evidence="ECO:0000259|PROSITE:PS51823"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1303..1348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1330..1348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1348 AA;  151047 MW;  35F1F2B587050EC6 CRC64;
     MVIKTDELPA AAPADSAREH GSQAGGKGRP SSAEPPSVML LNGDCSDSFK KEEGTAKPPR
     ENGLDEGEPG DETTGQEVIV IQDTGFSVKI LAPGIEPFSL QVSPQEMVQE IHQVLMDRED
     TCHRTCFSLH LDGNMLDHFS ELRSVEGLQE GSVLRVVEEP YTVREARIHV RHVRDLLKSL
     DPSDAFNGVD CNSLSFLSVF TDGDLGDSGK RKKGLEMDPI DCTPPEYILP GSRERPLCPL
     QPQNRDWKPL QCLKVLTMSG WNPPPGNRKM HGDLMYLFVI TAEDRQVSIT ASTRGFYLNQ
     STAYHFNPKP ASPRFLSHSL VELLNQISPT FKKNFAVLQK KRVQRHPFER IATPFQVYSW
     TAPQAEHAMD CVRAEDAYTS RLGYEEHIPG QTRDWNEELQ TTRELPRKNL PERLLRERAI
     FKVHSDFTAA ATRGAMAVID GNVMAINPSE ETKMQMFIWN NIFFSLGFDV RDHYKDFGGD
     VAAYVAPTND LNGVRTYNAV DVEGLYTLGT VVVDYRGYRV TAQSIIPGIL ERDQEQSVIY
     GSIDFGKTVV SHPRYLELLE RTSRPLKILR HRVLNDRDEE VELCSSVECK GIIGNDGRHY
     ILDLLRTFPP DLNFLPVPGE ELPEECTRAG FPRAHRHKLC CLRQELVDAF VEHRYLLFMK
     LAALQLMQQK ASKVETPTSL ENGGPPSSAE AESEDSVGPE AGSEEEGSSV SGLAKVKELA
     ETIASDDGTD PRSREVIRNA CKAVGSISST AFDIRFNPDI FSPGVRFPES CQDEVRDQKQ
     LLKDAAAFLL SCQIPGLVKD CTEHAVLPMD GATLAEVMRQ RGINMRYLGK VLDLVLRSPA
     RDQLDHIYKI GIGELITRSA KHIFKTYLQG VELSGLSAAI SHFLNCFLSS YPNPVAHLPA
     DELLSKKRNK RRKNRPPGAA DNTAWAVMTP QELWKNICQE AKNYFDFTLE CDSVDQAVET
     YGLQKITLLR EISLKTGIQI LLKEYSFDSR HKPAFTEEDV LNIFPVVKHV NPKASDAFHF
     FQSGQAKVQQ GFLKEGCELI NEALNLFNNV YGAMHVEICA CLRLLARLHY IMGDYAEALS
     NQQKAVLMSE RVMGIEHPNT IQEYMHLALY CFASSQLSTA LSLLYRARYL MLLVFGEDHP
     EMALLDNNIG LVLHGVMEYD LSLRFLENAL AVTTKYHGPK ALKVALSHHL VARVYESKAE
     FRAALQHEKE GYTIYKTQLG EDHEKTRESS EYLKCLTQQA VALQRTMNEI YRNGSSANIP
     PLKFTAPSMA SVLEQLNVIN GILFIPLSQK DLENLKAEVA RRHQLQEASR NRDKADDVAT
     DPEPARAQQE DMGSPQTAKE DPSLSLQG
//
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