S22AG_XENLA
ID S22AG_XENLA Reviewed; 566 AA.
AC Q66KG0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Solute carrier family 22 member 16;
DE AltName: Full=Carnitine transporter 2;
DE Short=CT2;
GN Name=slc22a16;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: High affinity carnitine transporter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; BC080416; AAH80416.1; -; mRNA.
DR AlphaFoldDB; Q66KG0; -.
DR SMR; Q66KG0; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..566
FT /note="Solute carrier family 22 member 16"
FT /id="PRO_0000318993"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 566 AA; 63754 MW; E3E5DCC2FAB656C0 CRC64;
MEHLFDYVGH FGRFQAYLYF ASAFQTISCG IHYLASVFIA VTPKFICRAP GNISTVLLPN
ASTLRLEDAW ESWTSKDYLV VQQENGDIWE LNQCSRLKRE DASYLTYFYD GNKTLFSCSN
GYHYDKSNLE SSIVTEWDLV CDREWLAKLI QPIFMLGVLI GAVIFGDIAD RVGRRPIIWI
TSTGQFLFGI AVAFTFDYYS FVIVRFLLAM VSSGYYVVVF VYLTEYVGIK ARTWASMHVH
AFFAVGVMIV SLVGFLVRTW WIYQIILSLT TLPFVLCCWM LPETPFWLYS QGKYKEVEKL
IRTIEKWNKI STPCKLSELC PAQETHVDQP NTLKNHNVLD LFYNWSFARR TITVWLIWFT
GSLGYYVFAL NSVNLGGNEY LNLFLTGAVE IPSYIVACLG MDKIGRRNTL APFLIISAVI
CGVIMLIPQD HSTVTIAMSM AGKFSIAVAF GLIYLYTAEL YPTIVRSLAV GSGSMMCRIG
SVVAPFCVYL TDVWIFMPQM LVGIMAFLTG ILTLTLPETL GIPLTSTMEE AAEMGTTSGI
TKRKALTESN GVVMEKLDQT TDNAAS