ID   GRP75_CANLF             Reviewed;          14 AA.
AC   P99502;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   11-DEC-2019, entry version 65.
DE   RecName: Full=Stress-70 protein, mitochondrial;
DE   AltName: Full=75 kDa glucose-regulated protein;
DE            Short=GRP-75;
DE   AltName: Full=Heat shock 70 kDa protein 9;
DE   Flags: Fragment;
GN   Name=HSPA9;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=9504812; DOI=10.1002/elps.1150181514;
RA   Dunn M.J., Corbett J.M., Wheeler C.H.;
RT   "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT   heart proteins.";
RL   Electrophoresis 18:2795-2802(1997).
CC   -!- FUNCTION: Chaperone protein which plays an important role in
CC       mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and
CC       stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU.
CC       Regulates erythropoiesis via stabilization of ISC assembly. May play a
CC       role in the control of cell proliferation and cellular aging.
CC       {ECO:0000250|UniProtKB:P38646, ECO:0000250|UniProtKB:P38647}.
CC   -!- SUBUNIT: Interacts strongly with the intermediate form of FXN and
CC       weakly with its mature form. Interacts with HSCB. Associates with the
CC       mitochondrial contact site and cristae organizing system (MICOS)
CC       complex, composed of at least MICOS10/MIC10, CHCHD3/MIC19,
CC       CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13.
CC       This complex was also known under the names MINOS or MitOS complex. The
CC       MICOS complex associates with mitochondrial outer membrane proteins
CC       SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein
CC       TMEM11 and with HSPA9. Interacts with DNLZ, the interaction is required
CC       to prevent self-aggregation. Interacts with TESPA1. Interacts with
CC       PDPN. Interacts with NFU1, NFS1 and ISCU.
CC       {ECO:0000250|UniProtKB:P38646}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P38646}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:P38646}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR   GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:1903707; P:negative regulation of hemopoiesis; ISS:UniProtKB.
DR   GO; GO:0045646; P:regulation of erythrocyte differentiation; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..>14
FT                   /note="Stress-70 protein, mitochondrial"
FT                   /id="PRO_0000078661"
FT   NON_TER         14
SQ   SEQUENCE   14 AA;  1440 MW;  2AAEDD1AACBAC8D8 CRC64;
     AXEAIFGAVV XIDL