ID S2533_BOVIN Reviewed; 321 AA.
AC Q1LZB3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Solute carrier family 25 member 33;
GN Name=SLC25A33;
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=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial transporter that imports/exports pyrimidine
CC nucleotides into and from mitochondria. Selectively transports uridine,
CC thymidine, guanosine, cytosine and inosine (deoxy)nucleoside di- and
CC triphosphates by an antiport mechanism (By similarity). May import
CC (deoxy)nucleoside triphosphates in exchange for intramitochondrial
CC (deoxy)nucleoside diphosphates, thus providing precursors necessary for
CC de novo synthesis of mitochondrial DNA and RNA while exporting products
CC of their catabolism (By similarity). Participates in mitochondrial
CC genome maintenance, regulation of mitochondrial membrane potential and
CC mitochondrial respiration (By similarity). Upon INS or IGF1 stimulation
CC regulates cell growth and proliferation by controlling mitochondrial
CC DNA replication and transcription, the ratio of mitochondria-to
CC nuclear-encoded components of the electron transport chain resulting in
CC control of mitochondrial ROS production (By similarity). Participates
CC in dendritic cell endocytosis and may associate with mitochondrial
CC oxidative phosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:Q9BSK2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP(out) + UTP(in) = UDP(in) + UTP(out); Xref=Rhea:RHEA:73515,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP(out) + UTP(in) = dUTP(in) + UTP(out);
CC Xref=Rhea:RHEA:73519, ChEBI:CHEBI:46398, ChEBI:CHEBI:61555;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=TTP(out) + UTP(in) = TTP(in) + UTP(out); Xref=Rhea:RHEA:73523,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:63527;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=TDP(out) + UTP(in) = TDP(in) + UTP(out); Xref=Rhea:RHEA:73527,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:61417;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP(out) + UTP(in) = CTP(in) + UTP(out); Xref=Rhea:RHEA:73531,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:46398;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP(out) + UTP(in) = CDP(in) + UTP(out); Xref=Rhea:RHEA:73535,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:58069;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCTP(out) + UTP(in) = dCTP(in) + UTP(out);
CC Xref=Rhea:RHEA:73539, ChEBI:CHEBI:46398, ChEBI:CHEBI:61481;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCDP(out) + UTP(in) = dCDP(in) + UTP(out);
CC Xref=Rhea:RHEA:73543, ChEBI:CHEBI:46398, ChEBI:CHEBI:58593;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP(out) + UTP(in) = GTP(in) + UTP(out); Xref=Rhea:RHEA:73547,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:46398;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP(out) + UTP(in) = GDP(in) + UTP(out); Xref=Rhea:RHEA:73551,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGTP(out) + UTP(in) = dGTP(in) + UTP(out);
CC Xref=Rhea:RHEA:73559, ChEBI:CHEBI:46398, ChEBI:CHEBI:61429;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGDP(out) + UTP(in) = dGDP(in) + UTP(out);
CC Xref=Rhea:RHEA:73563, ChEBI:CHEBI:46398, ChEBI:CHEBI:58595;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ITP(out) + UTP(in) = ITP(in) + UTP(out); Xref=Rhea:RHEA:73567,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:61402;
CC Evidence={ECO:0000250|UniProtKB:Q9BSK2};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9BSK2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; BC116108; AAI16109.1; -; mRNA.
DR RefSeq; XP_010811602.1; XM_010813300.1.
DR RefSeq; XP_010821400.1; XM_010823098.2.
DR AlphaFoldDB; Q1LZB3; -.
DR SMR; Q1LZB3; -.
DR STRING; 9913.ENSBTAP00000004127; -.
DR PaxDb; 9913-ENSBTAP00000004127; -.
DR Ensembl; ENSBTAT00000004127.6; ENSBTAP00000004127.5; ENSBTAG00000003177.6.
DR GeneID; 533794; -.
DR KEGG; bta:533794; -.
DR CTD; 84275; -.
DR VEuPathDB; HostDB:ENSBTAG00000003177; -.
DR VGNC; VGNC:34759; SLC25A33.
DR eggNOG; KOG0757; Eukaryota.
DR GeneTree; ENSGT00940000158954; -.
DR HOGENOM; CLU_015166_6_0_1; -.
DR InParanoid; Q1LZB3; -.
DR OMA; AFYNGMG; -.
DR OrthoDB; 4772at2759; -.
DR TreeFam; TF314220; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000003177; Expressed in retina and 104 other cell types or tissues.
DR ExpressionAtlas; Q1LZB3; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0015218; F:pyrimidine nucleotide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; ISS:UniProtKB.
DR GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; ISS:UniProtKB.
DR GO; GO:0006390; P:mitochondrial transcription; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1990519; P:pyrimidine nucleotide import into mitochondrion; ISS:UniProtKB.
DR GO; GO:0006864; P:pyrimidine nucleotide transport; ISS:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISS:UniProtKB.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR049562; SLC25A33/36-like.
DR PANTHER; PTHR45829; MITOCHONDRIAL CARRIER PROTEIN RIM2; 1.
DR PANTHER; PTHR45829:SF5; SOLUTE CARRIER FAMILY 25 MEMBER 33; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Solute carrier family 25 member 33"
FT /id="PRO_0000291784"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..65
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 9..118
FT /note="Solcar 1"
FT REPEAT 126..213
FT /note="Solcar 2"
FT REPEAT 231..315
FT /note="Solcar 3"
SQ SEQUENCE 321 AA; 35378 MW; 88FED5CFB45CE1EE CRC64;
MATGTQQKEN TLLHLFAGGC GGTVGAIFTC PLEVIKTRLQ SSRLALRTVY YPQVHLGTIS
GAGVVRQTSV TPGLLQVLKS ILEKEGPRSL FRGLGPNLVG VAPSRAVYFA CYSKAKEQFN
GVFVPNSNIV HVFSAGSAAF VTNSLMNPIW MVKTRMQLER KVRGSKQMNT LQCARYVYQT
EGIRGFYRGL TASYAGISET IICFAIYESL KKYLKEAPLA SSTNGTEKNS TNFFGLMAAA
ALSKGCASCV AYPHEVIRTR LREEGSKYKS FVQTARLVFR EEGYLAFYRG LFAQLIRQIP
NTAIVLSTYE LIVYLLEDHA Q
//
