CRC1_YEAST
ID CRC1_YEAST Reviewed; 327 AA.
AC Q12289; D6W2G1;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mitochondrial carnitine carrier;
GN Name=CRC1; OrderedLocusNames=YOR100C; ORFNames=YOR3193C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=10622748; DOI=10.1016/s0014-5793(99)01555-0;
RA Palmieri L., Lasorsa F.M., Iacobazzi V., Runswick M.J., Palmieri F.,
RA Walker J.E.;
RT "Identification of the mitochondrial carnitine carrier in Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 462:472-476(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION IN CARNITINE TRANSPORT.
RX PubMed=10545096; DOI=10.1093/emboj/18.21.5843;
RA van Roermund C.W., Hettema E.H., van den Berg M., Tabak H.F., Wanders R.J.;
RT "Molecular characterization of carnitine-dependent transport of acetyl-CoA
RT from peroxisomes to mitochondria in Saccharomyces cerevisiae and
RT identification of a plasma membrane carnitine transporter, Agp2p.";
RL EMBO J. 18:5843-5852(1999).
CC -!- FUNCTION: Transports carnitine, acetylcarnitine, propionylcarnitine and
CC to a much lower extent medium- and long-chain acylcarnitines.
CC {ECO:0000269|PubMed:10545096, ECO:0000269|PubMed:10622748}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ250124; CAB64359.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64022.1; -; Genomic_DNA.
DR EMBL; Z75008; CAA99297.1; -; Genomic_DNA.
DR EMBL; AY693195; AAT93214.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10877.1; -; Genomic_DNA.
DR PIR; S61660; S61660.
DR RefSeq; NP_014743.1; NM_001183519.1.
DR AlphaFoldDB; Q12289; -.
DR SMR; Q12289; -.
DR BioGRID; 34498; 105.
DR DIP; DIP-4154N; -.
DR IntAct; Q12289; 3.
DR MINT; Q12289; -.
DR STRING; 4932.YOR100C; -.
DR TCDB; 2.A.29.8.4; the mitochondrial carrier (mc) family.
DR UCD-2DPAGE; Q12289; -.
DR MaxQB; Q12289; -.
DR PaxDb; Q12289; -.
DR PRIDE; Q12289; -.
DR EnsemblFungi; YOR100C_mRNA; YOR100C; YOR100C.
DR GeneID; 854267; -.
DR KEGG; sce:YOR100C; -.
DR SGD; S000005626; CRC1.
DR VEuPathDB; FungiDB:YOR100C; -.
DR eggNOG; KOG0758; Eukaryota.
DR GeneTree; ENSGT00940000167609; -.
DR HOGENOM; CLU_015166_16_0_1; -.
DR InParanoid; Q12289; -.
DR OMA; QYTIGQI; -.
DR BioCyc; YEAST:G3O-33633-MON; -.
DR Reactome; R-SCE-200425; Carnitine metabolism.
DR PRO; PR:Q12289; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12289; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015227; F:acyl carnitine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005476; F:carnitine:acyl carnitine antiporter activity; IDA:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1902603; P:carnitine transmembrane transport; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:SGD.
DR GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..327
FT /note="Mitochondrial carnitine carrier"
FT /id="PRO_0000090681"
FT TRANSMEM 33..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..123
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..162
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..212
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..260
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 33..126
FT /note="Solcar 1"
FT REPEAT 139..221
FT /note="Solcar 2"
FT REPEAT 237..321
FT /note="Solcar 3"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 34754 MW; 0CF982E858BD1EA5 CRC64;
MSSDTSLSES SLLKEESGSL TKSRPPIKSN PVRENIKSFV AGGVGGVCAV FTGHPFDLIK
VRCQNGQANS TVHAITNIIK EAKTQVKGTL FTNSVKGFYK GVIPPLLGVT PIFAVSFWGY
DVGKKLVTFN NKQGGSNELT MGQMAAAGFI SAIPTTLVTA PTERVKVVLQ TSSKGSFIQA
AKTIVKEGGI ASLFKGSLAT LARDGPGSAL YFASYEISKN YLNSRQPRQD AGKDEPVNIL
NVCLAGGIAG MSMWLAVFPI DTIKTKLQAS STRQNMLSAT KEIYLQRGGI KGFFPGLGPA
LLRSFPANAA TFLGVEMTHS LFKKYGI