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Protein

Solute carrier family 22 member 4

Gene

Slc22a4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Sodium-ion dependent, low affinity carnitine transporter. Probably transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 1.78.1 Publication

pH dependencei

Optimum pH is 8.0. At higher pH, transport activity decreases.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi218 – 225ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • organic cation transmembrane transporter activity Source: RGD
  • quaternary ammonium group transmembrane transporter activity Source: RGD
  • symporter activity Source: UniProtKB-KW

GO - Biological processi

  • quaternary ammonium group transport Source: RGD
  • sodium ion transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ion transport, Sodium transport, Symport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 22 member 4
Alternative name(s):
Organic cation/carnitine transporter 1
Gene namesi
Name:Slc22a4
Synonyms:Octn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621149. Slc22a4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 20CytoplasmicSequence analysisAdd BLAST20
Transmembranei21 – 41Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini42 – 142ExtracellularSequence analysisAdd BLAST101
Transmembranei143 – 163Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini164 – 171CytoplasmicSequence analysis8
Transmembranei172 – 192Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini193 – 197ExtracellularSequence analysis5
Transmembranei198 – 218Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini219 – 232CytoplasmicSequence analysisAdd BLAST14
Transmembranei233 – 253Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini254 – 257ExtracellularSequence analysis4
Transmembranei258 – 278Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini279 – 339CytoplasmicSequence analysisAdd BLAST61
Transmembranei340 – 360Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini361 – 373ExtracellularSequence analysisAdd BLAST13
Transmembranei374 – 394Helical; Name=8Sequence analysisAdd BLAST21
Topological domaini395 – 400CytoplasmicSequence analysis6
Transmembranei401 – 421Helical; Name=9Sequence analysisAdd BLAST21
Topological domaini422 – 428ExtracellularSequence analysis7
Transmembranei429 – 449Helical; Name=10Sequence analysisAdd BLAST21
Topological domaini450 – 462CytoplasmicSequence analysisAdd BLAST13
Transmembranei463 – 483Helical; Name=11Sequence analysisAdd BLAST21
Topological domaini484 – 488ExtracellularSequence analysis5
Transmembranei489 – 509Helical; Name=12Sequence analysisAdd BLAST21
Topological domaini510 – 553CytoplasmicSequence analysisAdd BLAST44

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2073667.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002204991 – 553Solute carrier family 22 member 4Add BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...)Sequence analysis1
Glycosylationi64N-linked (GlcNAc...)Sequence analysis1
Glycosylationi91N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9R141.
PRIDEiQ9R141.

PTM databases

iPTMnetiQ9R141.
PhosphoSitePlusiQ9R141.

Expressioni

Tissue specificityi

Expressed in intestine, liver and kidney. Weakly expressed in brain, thymus, lung, spleen, heart and skin. In brain, it is expressed in cerebellum, especially in the granular layer, in hippocampus and cortex. In kidney, it is expressed in cortex and medulla with relatively more abundance in the cortical-medullary junction. In heart, it is expressed in myocardium and valves. Expressed labyrinthine zone of the placenta.1 Publication

Interactioni

Subunit structurei

Interacts with PDZK1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055693.

Structurei

3D structure databases

ProteinModelPortaliQ9R141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0255. Eukaryota.
COG0477. LUCA.
HOVERGENiHBG061545.
InParanoidiQ9R141.
KOiK08202.
PhylomeDBiQ9R141.

Family and domain databases

CDDicd06174. MFS. 1 hit.
InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport-like.
IPR004749. Orgcat_transp/SVOP.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00898. 2A0119. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R141-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRDYDEVIAF LGDWGPFQRL IFFLLSASII PNGFNGMSVV FLAGTPEHRC
60 70 80 90 100
LVPHTVNLSS AWRNHSIPLE TKDGRQVPQS CRRYRLATIA NFSALGLEPG
110 120 130 140 150
LDVDLEQLEQ ESCLDGWEYS KDVFLSTIVT EWNLVCEDDW KTPLTTSLFF
160 170 180 190 200
VGVLCGSFVS GQLSDRFGRK KVLFATMAVQ TGFSFVQIFS TNWEMFTVLF
210 220 230 240 250
AIVGMGQISN YVVAFILGTE ILSKSVRILF STLGVCTFFA IGYMVLPLFA
260 270 280 290 300
YFIRDWRMLL LALTLPGLFC VPLWWFIPES PRWLISQRRF EEAEQIIQKA
310 320 330 340 350
AKMNGIMAPA VIFDPLELQE LNSLKQQKVF ILDLFKTRNI ATITVMSVML
360 370 380 390 400
WMLTSVGYFA LSLNVPNLHG DVYLNCFLSG LIEVPAYFTA WLLLRTLPRR
410 420 430 440 450
YIIAGVLFWG GGVLLLVQVV PEDYNFVSIG LVMLGKFGVT SAFSMLYVFT
460 470 480 490 500
AELYPTLVRN MAVGITSMAS RVGSIIAPYF VYLGAYNRLL PYILMGSLTV
510 520 530 540 550
LIGIITLFFP ESFGVTLPEN LEQMQKVRGF RCGKKSTVSM DREENPKVLI

TAF
Length:553
Mass (Da):62,362
Last modified:May 1, 2000 - v1
Checksum:iE26C8155768A14AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169831 mRNA. Translation: AAD46922.1.
RefSeqiNP_071606.1. NM_022270.1.
UniGeneiRn.163093.

Genome annotation databases

GeneIDi64037.
KEGGirno:64037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169831 mRNA. Translation: AAD46922.1.
RefSeqiNP_071606.1. NM_022270.1.
UniGeneiRn.163093.

3D structure databases

ProteinModelPortaliQ9R141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055693.

Chemistry databases

ChEMBLiCHEMBL2073667.

PTM databases

iPTMnetiQ9R141.
PhosphoSitePlusiQ9R141.

Proteomic databases

PaxDbiQ9R141.
PRIDEiQ9R141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64037.
KEGGirno:64037.

Organism-specific databases

CTDi6583.
RGDi621149. Slc22a4.

Phylogenomic databases

eggNOGiKOG0255. Eukaryota.
COG0477. LUCA.
HOVERGENiHBG061545.
InParanoidiQ9R141.
KOiK08202.
PhylomeDBiQ9R141.

Miscellaneous databases

PROiQ9R141.

Family and domain databases

CDDicd06174. MFS. 1 hit.
InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport-like.
IPR004749. Orgcat_transp/SVOP.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00898. 2A0119. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiS22A4_RAT
AccessioniPrimary (citable) accession number: Q9R141
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Inhibited by desipramin > DMA > procainamide > cimetidine.

Caution

It is unclear whether it transports carnitine in vivo.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.