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TIM9_CHICK
ID   TIM9_CHICK              Reviewed;          89 AA.
AC   Q5ZIR8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN   Name=TIMM9; Synonyms=TIM9; ORFNames=RCJMB04_23p13;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC       the import and insertion of multi-pass transmembrane proteins into the
CC       mitochondrial inner membrane. May also be required for the transfer of
CC       beta-barrel precursors from the TOM complex to the sorting and assembly
CC       machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC       protein that protects the hydrophobic precursors from aggregation and
CC       guide them through the mitochondrial intermembrane space (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of
CC       TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-
CC       bladed alpha-propeller structure and associates with the TIMM22
CC       component of the TIM22 complex. Interacts with multi-pass transmembrane
CC       proteins in transit (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC       {ECO:0000250}.
CC   -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC       2 disulfide bonds in the mitochondrial intermembrane space. However,
CC       during the transit of TIMM9 from cytoplasm into mitochondrion, the Cys
CC       residues probably coordinate zinc, thereby preventing folding and
CC       allowing its transfer across mitochondrial outer membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR   EMBL; AJ720716; CAG32375.1; -; mRNA.
DR   RefSeq; NP_001258083.1; NM_001271154.1.
DR   RefSeq; NP_001258084.1; NM_001271155.1.
DR   RefSeq; XP_015142737.1; XM_015287251.1.
DR   RefSeq; XP_015142738.1; XM_015287252.1.
DR   RefSeq; XP_015142739.1; XM_015287253.1.
DR   AlphaFoldDB; Q5ZIR8; -.
DR   SMR; Q5ZIR8; -.
DR   PaxDb; Q5ZIR8; -.
DR   Ensembl; ENSGALT00000089409; ENSGALP00000058891; ENSGALG00000031966.
DR   GeneID; 100859762; -.
DR   KEGG; gga:100859762; -.
DR   CTD; 26520; -.
DR   VEuPathDB; HostDB:geneid_100859762; -.
DR   GeneTree; ENSGT00940000165313; -.
DR   InParanoid; Q5ZIR8; -.
DR   OMA; QDFLRMY; -.
DR   OrthoDB; 1627953at2759; -.
DR   PhylomeDB; Q5ZIR8; -.
DR   TreeFam; TF106192; -.
DR   PRO; PR:Q5ZIR8; -.
DR   Proteomes; UP000000539; Chromosome 5.
DR   Bgee; ENSGALG00000031966; Expressed in colon and 12 other tissues.
DR   ExpressionAtlas; Q5ZIR8; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.810; -; 1.
DR   InterPro; IPR004217; Tim10-like.
DR   InterPro; IPR035427; Tim10-like_dom_sf.
DR   Pfam; PF02953; zf-Tim10_DDP; 1.
DR   SUPFAM; SSF144122; SSF144122; 1.
PE   3: Inferred from homology;
KW   Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Reference proteome;
KW   Translocation; Transport; Zinc.
FT   CHAIN           1..89
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim9"
FT                   /id="PRO_0000228035"
FT   MOTIF           28..52
FT                   /note="Twin CX3C motif"
FT   DISULFID        28..52
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..48
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   89 AA;  10483 MW;  D3AA84333C8DABA0 CRC64;
     MAGQISETDQ IKQFKEFLGT YNKITENCFM DCIRDFTTRE VKPEEITCSE HCLQKYLKMT
     QRISMRFQEY HIQQNEALAA KAGLLSQPR
 
 
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