MOT9_CHICK
ID MOT9_CHICK Reviewed; 507 AA.
AC Q5ZJU0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Monocarboxylate transporter 9;
DE Short=MCT 9;
DE AltName: Full=Solute carrier family 16 member 9;
GN Name=SLC16A9; Synonyms=MCT9; ORFNames=RCJMB04_15m4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the
CC rapid transport across the plasma membrane of many monocarboxylates (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR EMBL; AJ720344; CAG32003.1; -; mRNA.
DR RefSeq; NP_001026393.1; NM_001031222.1.
DR AlphaFoldDB; Q5ZJU0; -.
DR SMR; Q5ZJU0; -.
DR STRING; 9031.ENSGALP00000005024; -.
DR PaxDb; Q5ZJU0; -.
DR GeneID; 423667; -.
DR KEGG; gga:423667; -.
DR CTD; 220963; -.
DR VEuPathDB; HostDB:geneid_423667; -.
DR eggNOG; KOG2504; Eukaryota.
DR InParanoid; Q5ZJU0; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; Q5ZJU0; -.
DR PRO; PR:Q5ZJU0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:1902603; P:carnitine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR030767; MCT9.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF158; PTHR11360:SF158; 1.
DR Pfam; PF07690; MFS_1; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..507
FT /note="Monocarboxylate transporter 9"
FT /id="PRO_0000289335"
FT TOPO_DOM 1..12
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..369
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 55944 MW; F10541993A40D560 CRC64;
MVYRKPPDGG WGWVIVIVSF FTQFLCYGSP LAVGVLYLEW LDAFGEGKGK TAWVGSLANG
IGLLASPVCS ICVSSFGARP VAIFSGFMVA GGLMMSSFAP NIYFLYLSYG IVVGLGCGLL
YNATVTITCQ YFDKRRGLAL GLISTGSSVG LFIYAALQRE LIELYGLDGC LLIVGALSLN
ILACGSLMRP LESSDSPSPE KACTDKVPDQ YFVYHEKEKT VEENISILEK GYIDEKCANN
VPDYKQDNIL NKNVLSSINV DEKDTYKKKV VEQTNFCKQL AKRKWQLYLN YWEETVVLFK
NRVFSALFFA ILLFDIGGFP PSLLMEDIAR SANINEEDYH MPLVSIIGIM TAIGKLILGI
LADFKWVNTL YLYVLTLLMM GAALLAIPFA RSYFTLAVLS GILGFLTGNW SIFPYVTTKT
VGIEKLTHAY GILMFFAGLG NSLGPPIVGW FYDWTQEYDT AFYFSGFCVL LGGFLLLLAA
LPCWNACTDR SSKLPPNTYS YKVASSA