ID DIF1_CAEEL Reviewed; 312 AA.
AC Q27257; Q20630;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Protein dif-1;
GN Name=dif-1; ORFNames=F49E8.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7803813; DOI=10.3109/10425179409020854;
RA Runswick M.J., Philippides A., Lauria G., Walker J.E.;
RT "Extension of the mitochondrial transporter super-family: sequences of five
RT members from the nematode worm, Caenorhabditis elegans.";
RL DNA Seq. 4:281-291(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7774589; DOI=10.1002/j.1460-2075.1995.tb07225.x;
RA Ahringer J.;
RT "Embryonic tissue differentiation in Caenorhabditis elegans requires dif-1,
RT a gene homologous to mitochondrial solute carriers.";
RL EMBO J. 14:2307-2316(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Seems to play a role in the maintenance of tissue
CC differentiation in the developing embryo, but not for its initiation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Although dif-1 activity is required only during
CC embryogenesis, it is expressed at all stages of development.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; X76115; CAA53721.1; -; mRNA.
DR EMBL; Z48240; CAA88283.1; -; Genomic_DNA.
DR EMBL; FO081280; CCD70447.1; -; Genomic_DNA.
DR PIR; T29640; T29640.
DR RefSeq; NP_501223.1; NM_068822.5.
DR AlphaFoldDB; Q27257; -.
DR SMR; Q27257; -.
DR BioGRID; 42648; 22.
DR IntAct; Q27257; 1.
DR STRING; 6239.F49E8.5.3; -.
DR TCDB; 2.A.29.8.2; the mitochondrial carrier (mc) family.
DR EPD; Q27257; -.
DR PaxDb; 6239-F49E8-5-2; -.
DR PeptideAtlas; Q27257; -.
DR EnsemblMetazoa; F49E8.5.1; F49E8.5.1; WBGene00000996.
DR EnsemblMetazoa; F49E8.5.2; F49E8.5.2; WBGene00000996.
DR UCSC; F49E8.5.1; c. elegans.
DR AGR; WB:WBGene00000996; -.
DR WormBase; F49E8.5; CE28408; WBGene00000996; dif-1.
DR eggNOG; KOG0758; Eukaryota.
DR GeneTree; ENSGT00940000167609; -.
DR HOGENOM; CLU_015166_16_0_1; -.
DR InParanoid; Q27257; -.
DR OMA; QQKCPED; -.
DR OrthoDB; 4064096at2759; -.
DR PhylomeDB; Q27257; -.
DR Reactome; R-CEL-200425; Carnitine metabolism.
DR PRO; PR:Q27257; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000996; Expressed in embryo and 6 other cell types or tissues.
DR GO; GO:0005740; C:mitochondrial envelope; IMP:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015227; F:acyl carnitine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR GO; GO:1902603; P:carnitine transmembrane transport; IBA:GO_Central.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro.
DR GO; GO:0006839; P:mitochondrial transport; IMP:UniProtKB.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR InterPro; IPR002113; ADT_euk_type.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45624:SF4; CONGESTED-LIKE TRACHEA PROTEIN-RELATED; 1.
DR PANTHER; PTHR45624; MITOCHONDRIAL BASIC AMINO ACIDS TRANSPORTER-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00927; ADPTRNSLCASE.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Developmental protein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..312
FT /note="Protein dif-1"
FT /id="PRO_0000090693"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 2..93
FT /note="Solcar 1"
FT REPEAT 102..193
FT /note="Solcar 2"
FT REPEAT 203..289
FT /note="Solcar 3"
SQ SEQUENCE 312 AA; 33135 MW; CCF1300CAE4DF64F CRC64;
MSDVLLNFIA GGVGGSCTVI VGHPFDTVKV RIQTMPMPKP GEKPQFTGAL DCVKRTVSKE
GFFALYKGMA APLVGVSPLF AVFFGGCAVG KWLQQTDPSQ EMTFIQNANA GALAGVFTTI
VMVPGERIKC LLQVQQAGSA GSGVHYDGPL DVVKKLYKQG GISSIYRGTG ATLLRDIPAS
AAYLSVYEYL KKKFSGEGAQ RTLSPGATLM AGGLAGIANW GVCIPADVLK SRLQTAPEGK
YPDGIRGVLR EVLREEGPRA LFKGFWPVML RAFPANAACF FGLELTLAAF RYFGIGGHPT
PSTEVVPLPH DE
//
