ID   DJC11_PONAB             Reviewed;         559 AA.
AC   Q5RC70;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=DnaJ homolog subfamily C member 11;
GN   Name=DNAJC11;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for mitochondrial inner membrane organization. Seems
CC       to function through its association with the MICOS complex and the
CC       mitochondrial outer membrane sorting assembly machinery (SAM) complex.
CC       {ECO:0000250|UniProtKB:Q5U458, ECO:0000250|UniProtKB:Q9NVH1}.
CC   -!- SUBUNIT: Associates with the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC       CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC       and QIL1/MIC13. This complex was also known under the names MINOS or
CC       MitOS complex. The MICOS complex associates with mitochondrial outer
CC       membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC       components of the mitochondrial outer membrane sorting assembly
CC       machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC       protein TMEM11 and with HSPA9. The MICOS and SAM complexes together
CC       with DNAJC11 are part of a large protein complex spanning both
CC       membranes termed the mitochondrial intermembrane space bridging (MIB)
CC       complex. {ECO:0000250|UniProtKB:Q9NVH1}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NVH1}.
CC       Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NVH1}; Peripheral
CC       membrane protein {ECO:0000250|UniProtKB:Q9NVH1}.
CC   -!- SIMILARITY: Belongs to the DNAJC11 family. {ECO:0000305}.
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DR   EMBL; CR858410; CAH90637.1; -; mRNA.
DR   RefSeq; NP_001125345.1; NM_001131873.1.
DR   AlphaFoldDB; Q5RC70; -.
DR   SMR; Q5RC70; -.
DR   STRING; 9601.ENSPPYP00000002243; -.
DR   Ensembl; ENSPPYT00000002310; ENSPPYP00000002243; ENSPPYG00000001934.
DR   GeneID; 100172247; -.
DR   KEGG; pon:100172247; -.
DR   CTD; 55735; -.
DR   eggNOG; KOG0718; Eukaryota.
DR   GeneTree; ENSGT00860000133842; -.
DR   HOGENOM; CLU_019611_2_0_1; -.
DR   InParanoid; Q5RC70; -.
DR   OrthoDB; 532187at2759; -.
DR   TreeFam; TF105170; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0061617; C:MICOS complex; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0001401; C:SAM complex; IEA:Ensembl.
DR   GO; GO:0042407; P:cristae formation; IEA:Ensembl.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR024586; DnaJ-like_C11_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF11875; DUF3395; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Coiled coil; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVH1"
FT   CHAIN           2..559
FT                   /note="DnaJ homolog subfamily C member 11"
FT                   /id="PRO_0000247159"
FT   DOMAIN          14..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   COILED          417..457
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVH1"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5U458"
SQ   SEQUENCE   559 AA;  63292 MW;  8DBFD10523344DEC CRC64;
     MATALSEEEL DNEDYYSLLN VRREASSEEL KAAYRRLCML YHPDKHRDPE LKSQAERLFN
     LVHQAYEVLS DPQTRAIYDI YGKRGLEMEG WEVVERRRTP AEIREEFERL QREREERRLQ
     QRTNPKGTIS VGVDATDLFD RYDEEYEDVS GSSFPQIEIN KMHISQSIEA PLTATDTAIL
     SGSLSTQNGN GGGSINFALR RVTSAKGWGE LEFGAGDLQG PLFGLKLFRN LTPRCFVTTN
     CALQFSSRGI RPGLTTVLAR NLDKNTVGYL QWRWGIQSAM NTSIVRDTKT SHFTVALQLG
     IPHSFALISY QHKFQDDDQT RVKGSLKAGF FGTVVEYGAE RKISRHSVLG AAVSIGVPQG
     VSLKVKLNRA SQTYFFPIHL TDQLLPSAVF YATMGPLVVY FAMHRLIIKP YLRAQKEKEL
     EKQRESAATD VLQKKQEAES AVRLMQESVR RIIEAEESRM GLIIVNAWYG KFVNDKSRKS
     EKVKVIDVTV PLQCLVKDSK LILTEASKAG LPGFYDPCVG EEKNLKVLYQ FRGVLHQVMV
     LDSEALRIPK QSHRIDTDG