ID   SDHF1_BOVIN             Reviewed;         118 AA.
AC   A8PU71;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Succinate dehydrogenase assembly factor 1, mitochondrial {ECO:0000250|UniProtKB:A6NFY7};
DE            Short=SDH assembly factor 1 {ECO:0000250|UniProtKB:A6NFY7};
DE            Short=SDHAF1 {ECO:0000250|UniProtKB:A6NFY7};
DE   AltName: Full=LYR motif-containing protein 8 {ECO:0000250|UniProtKB:A6NFY7};
GN   Name=SDHAF1 {ECO:0000250|UniProtKB:A6NFY7};
GN   Synonyms=LYRM8 {ECO:0000250|UniProtKB:A6NFY7};
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=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an essential role in the assembly of succinate
CC       dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC       complex II) that is a component of both the tricarboxylic acid (TCA)
CC       cycle and the mitochondrial electron transport chain, and which couples
CC       the oxidation of succinate to fumarate with the reduction of ubiquinone
CC       (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur
CC       protein subunit SDHB of the SDH catalytic dimer, protecting it from the
CC       deleterious effects of oxidants. May act together with SDHAF3.
CC       Contributes to iron-sulfur cluster incorporation into SDHB by binding
CC       to SDHB and recruiting the iron-sulfur transfer complex formed by
CC       HSC20, HSPA9 and ISCU through direct binding to HSC20.
CC       {ECO:0000250|UniProtKB:A6NFY7}.
CC   -!- SUBUNIT: Interacts with SDHB within an SDHA-SDHB subcomplex. Also
CC       interacts with the iron-sulfur transfer complex formed by HSC20, HSPA9
CC       and ISCU through direct binding to HSC20. Binding of SDHAF1 to SDHB
CC       precedes and is necessary for recruitment of the iron-sulfur transfer
CC       complex by SDHAF1. {ECO:0000250|UniProtKB:Q3E785}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:A6NFY7}.
CC   -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC112496; AAI12497.1; -; mRNA.
DR   RefSeq; NP_001103912.1; NM_001110442.2.
DR   AlphaFoldDB; A8PU71; -.
DR   SMR; A8PU71; -.
DR   STRING; 9913.ENSBTAP00000050423; -.
DR   PaxDb; A8PU71; -.
DR   PRIDE; A8PU71; -.
DR   Ensembl; ENSBTAT00000055698; ENSBTAP00000050423; ENSBTAG00000037461.
DR   GeneID; 784051; -.
DR   KEGG; bta:784051; -.
DR   CTD; 644096; -.
DR   VEuPathDB; HostDB:ENSBTAG00000037461; -.
DR   VGNC; VGNC:34389; SDHAF1.
DR   eggNOG; KOG4620; Eukaryota.
DR   GeneTree; ENSGT00940000157289; -.
DR   HOGENOM; CLU_154777_0_1_1; -.
DR   InParanoid; A8PU71; -.
DR   OMA; FRENARI; -.
DR   OrthoDB; 1638205at2759; -.
DR   TreeFam; TF344152; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000037461; Expressed in prostate gland and 105 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; ISS:UniProtKB.
DR   CDD; cd20268; Complex1_LYR_SDHAF1_LYRM8; 1.
DR   InterPro; IPR008011; Complex1_LYR_dom.
DR   InterPro; IPR045295; Complex1_LYR_SDHAF1_LYRM8.
DR   Pfam; PF05347; Complex1_LYR; 1.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome; Repeat.
FT   CHAIN           1..118
FT                   /note="Succinate dehydrogenase assembly factor 1,
FT                   mitochondrial"
FT                   /id="PRO_0000327915"
FT   REGION          53..65
FT                   /note="Interaction with SDHB"
FT                   /evidence="ECO:0000250|UniProtKB:A6NFY7"
FT   REGION          72..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           14..16
FT                   /note="LYR motif 1; required for interaction with HSC20"
FT                   /evidence="ECO:0000250|UniProtKB:A6NFY7"
FT   MOTIF           53..55
FT                   /note="LYR motif 2; not required for interaction with
FT                   HSC20"
FT                   /evidence="ECO:0000250|UniProtKB:A6NFY7"
SQ   SEQUENCE   118 AA;  13253 MW;  CA5D10FC5D676AA1 CRC64;
     MSRHSRLQRQ VLSLYRELLR AGRGKPGAEA RVRAEFRQHA CLPRSDVLRI EYLYRRGRRQ
     LQMLRSGHAT AMGAFVRTRG PTEESNGAGA PGTLSGEGDD PRKPLDSMRT PKTPLDGR