S22AG_MOUSE
ID S22AG_MOUSE Reviewed; 649 AA.
AC Q497L8; Q3LVC1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Solute carrier family 22 member 16;
DE AltName: Full=Carnitine transporter 2;
DE Short=CT2;
GN Name=Slc22a16;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Testis;
RA Fisher D.J., Lye R.J., Hinton B.T.;
RT "Mouse carnitine transporter 2.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: High affinity carnitine transporter; the uptake is partially
CC sodium-ion dependent. Thought to mediate the L-carnitine secretion
CC mechanism from testis epididymal epithelium into the lumen which is
CC involved in the maturation of spermatozoa. Also transports organic
CC cations such as tetraethylammonium (TEA) and doxorubicin. The uptake of
CC TEA is inhibited by various organic cations. The uptake of doxorubicin
CC is sodium-independent (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q497L8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q497L8-2; Sequence=VSP_031339;
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR EMBL; DQ164804; ABA10822.1; -; mRNA.
DR EMBL; DQ164805; ABA10823.1; -; mRNA.
DR EMBL; BC100473; AAI00474.1; -; mRNA.
DR CCDS; CCDS23796.1; -. [Q497L8-1]
DR RefSeq; NP_081848.1; NM_027572.1. [Q497L8-1]
DR AlphaFoldDB; Q497L8; -.
DR SMR; Q497L8; -.
DR STRING; 10090.ENSMUSP00000077428; -.
DR GlyGen; Q497L8; 3 sites.
DR PhosphoSitePlus; Q497L8; -.
DR PaxDb; Q497L8; -.
DR PRIDE; Q497L8; -.
DR ProteomicsDB; 260888; -. [Q497L8-1]
DR ProteomicsDB; 260889; -. [Q497L8-2]
DR Antibodypedia; 32327; 117 antibodies from 23 providers.
DR DNASU; 70840; -.
DR Ensembl; ENSMUST00000019978; ENSMUSP00000019978; ENSMUSG00000019834. [Q497L8-2]
DR Ensembl; ENSMUST00000078314; ENSMUSP00000077428; ENSMUSG00000019834. [Q497L8-1]
DR GeneID; 70840; -.
DR KEGG; mmu:70840; -.
DR UCSC; uc007ewz.1; mouse. [Q497L8-1]
DR CTD; 85413; -.
DR MGI; MGI:1918090; Slc22a16.
DR VEuPathDB; HostDB:ENSMUSG00000019834; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000160723; -.
DR HOGENOM; CLU_001265_33_4_1; -.
DR InParanoid; Q497L8; -.
DR OMA; TEVYQSI; -.
DR PhylomeDB; Q497L8; -.
DR TreeFam; TF315847; -.
DR Reactome; R-MMU-549127; Organic cation transport.
DR BioGRID-ORCS; 70840; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q497L8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q497L8; protein.
DR Bgee; ENSMUSG00000019834; Expressed in spermatid and 90 other tissues.
DR ExpressionAtlas; Q497L8; baseline and differential.
DR Genevisible; Q497L8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005275; F:amine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; ISO:MGI.
DR GO; GO:0046717; P:acid secretion; ISO:MGI.
DR GO; GO:0015879; P:carnitine transport; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:MGI.
DR GO; GO:0015695; P:organic cation transport; ISO:MGI.
DR GO; GO:0007338; P:single fertilization; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..649
FT /note="Solute carrier family 22 member 16"
FT /id="PRO_0000318992"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 530..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..18
FT /note="MESCNVELIFDHIGHFGR -> MHKSGQQPMTWLVLLSIGHRRRRTLLGLGR
FT CRQYSHPFG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_031339"
SQ SEQUENCE 649 AA; 73933 MW; 94BF1C8E7C6733FE CRC64;
MESCNVELIF DHIGHFGRFQ IVLYLICAYQ SLSCGIHYLS SVFLSIIPEH ACKPPGMVRK
AVFHNVSAWR LEDILALRSP EHKDHIMVEL QDGEIWELTR CSRTWRENTS HLGYEYSGYK
HDSPCFDGYV YDQSKWRNSA VRNFNLVCDQ KWYARMIQPL IIFGVMLGSI TFSYLSDRFG
RRMALWCTSI GVFFFGIASL FIFDYLSFMI TRFFLVMASS GYFVVVFVYV MEIIGKKART
WASIHLNTFF AIGAMLVALA SYLLKTWWLY QIILCIVTTP FILCCWMLPE TPFWLLSEGR
YKEAQGTVDT MAVWNKSSSC DLVELLSLDV TRSHNKSPHS IRKHRLADLF HNLDVAKMTL
IVWLDWFTAN LGYYMFGKEV IRRKENEPLY LLLVGAMEIP AYICLCIWLK RVGRRKTMLL
FLLVSSLTCM LHVVMPSDYK TAKRMVALLV KSVISSVFAF IYLYTAELYP TTVRCLAVGS
SNMVSHVSSI FIPFTSHFSK VWIFLPQILF GILAILSGLL SLKLPETQDT PMKSTWETTE
QQVPENKDSL GEGPPDSFER WDSSRALSFA ERWGLSRASP DAEKWGSGRV PPDAGKWGAG
IAPPVTERGA SGRASLEDES GGSGRAPPEK NTEMENEIEN MKVSNLGGF
