ID   DJC11_BOVIN             Reviewed;         559 AA.
AC   Q2NL21;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DnaJ homolog subfamily C member 11;
GN   Name=DNAJC11;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) 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; BC111191; AAI11192.1; -; mRNA.
DR   RefSeq; NP_001039458.1; NM_001045993.1.
DR   AlphaFoldDB; Q2NL21; -.
DR   SMR; Q2NL21; -.
DR   STRING; 9913.ENSBTAP00000014899; -.
DR   PaxDb; Q2NL21; -.
DR   PRIDE; Q2NL21; -.
DR   Ensembl; ENSBTAT00000014899; ENSBTAP00000014899; ENSBTAG00000011217.
DR   GeneID; 508137; -.
DR   KEGG; bta:508137; -.
DR   CTD; 55735; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011217; -.
DR   eggNOG; KOG0718; Eukaryota.
DR   GeneTree; ENSGT00860000133842; -.
DR   HOGENOM; CLU_019611_2_0_1; -.
DR   InParanoid; Q2NL21; -.
DR   OMA; SMSTQID; -.
DR   OrthoDB; 532187at2759; -.
DR   TreeFam; TF105170; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000011217; Expressed in choroid plexus and 107 other tissues.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042407; P:cristae formation; IBA:GO_Central.
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_0000247156"
FT   DOMAIN          14..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   COILED          418..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;  63237 MW;  39B8AED7CC4B1E21 CRC64;
     MATALSEEEL DNEDYYSLLN VRREASCEEL KAAYRRLCML YHPDKHRDPE LKSQAERLFN
     LVHQAYEVLS DPQTRAIYDI YGKRGLEMEG WEVVERRRTP AEIREEFERL QREREERRLQ
     QRTNPKGTIS VGIDATDLFD RYEEEYEDVS GSGFPQIEIN KMHISQSIEA PLTASDTAIL
     SGSLSTQNGN GGGSINFALR RVTSAKGWGE LEFGAGDLQG PLFGLKLFRN LTPRCFVTTH
     CALQFSSRGI RPGLTTVLAR NLDKNTVGYL QWRWGVQSAM NTSIVRDTKT SHFTVALQLG
     IPHSFALISY QHKFQDDDQT RVKGSLKAGF FGTVVEYGAE RKISRHSVLG AAVSIGVPQG
     VSLKIKLNRA SQTYFFPIHL TDQLLPSAVF YATAGPLVLY FALHRLVIRP YLRAQKEKEL
     EKQRESTATD ILQKKQEAEA AVRLMQESVR RIIEAEESRM GLIIVNAWYG KFVNDKSKKS
     EKVKVIDVTV PLQCLVKDSK LILTEASKAG LPGFYDPCVG EEKNLKVLYQ FRGVLHQVMA
     LDSEALRIPK QSHRIDTDG