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Protein

Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+)

Gene

Slc6a14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na+/Cl--dependent manner.2 Publications

GO - Molecular functioni

  • amine transmembrane transporter activity Source: MGI
  • neurotransmitter:sodium symporter activity Source: InterPro

GO - Biological processi

  • amine transport Source: GOC
  • amino acid transport Source: UniProtKB-KW
  • response to toxic substance Source: MGI
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Symport, Transport

Enzyme and pathway databases

ReactomeiREACT_301178. Amino acid transport across the plasma membrane.
REACT_307956. Na+/Cl- dependent neurotransmitter transporters.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+)
Alternative name(s):
Amino acid transporter ATB0+
Colonic system B0+ amino acid transporter CATB0+
Solute carrier family 6 member 14
Gene namesi
Name:Slc6a14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1890216. Slc6a14.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei45 – 6521Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei72 – 9221Helical; Name=2Sequence AnalysisAdd
BLAST
Transmembranei110 – 13021Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini131 – 230100ExtracellularSequence AnalysisAdd
BLAST
Transmembranei231 – 25121Helical; Name=4Sequence AnalysisAdd
BLAST
Transmembranei257 – 27721Helical; Name=5Sequence AnalysisAdd
BLAST
Transmembranei311 – 33121Helical; Name=6Sequence AnalysisAdd
BLAST
Transmembranei344 – 36421Helical; Name=7Sequence AnalysisAdd
BLAST
Transmembranei395 – 41521Helical; Name=8Sequence AnalysisAdd
BLAST
Transmembranei453 – 47321Helical; Name=9Sequence AnalysisAdd
BLAST
Transmembranei476 – 49621Helical; Name=10Sequence AnalysisAdd
BLAST
Transmembranei524 – 54421Helical; Name=11Sequence AnalysisAdd
BLAST
Transmembranei559 – 57921Helical; Name=12Sequence AnalysisAdd
BLAST
Topological domaini580 – 63859CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • brush border membrane Source: Ensembl
  • extracellular exosome Source: MGI
  • integral component of plasma membrane Source: MGI
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+)PRO_0000214796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9JMA9.

PTM databases

PhosphoSiteiQ9JMA9.

Expressioni

Tissue specificityi

Expressed in the distal region of the intestinal tract: cecum and colon.2 Publications

Gene expression databases

BgeeiQ9JMA9.
ExpressionAtlasiQ9JMA9. baseline and differential.
GenevisibleiQ9JMA9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033414.

Structurei

3D structure databases

ProteinModelPortaliQ9JMA9.
SMRiQ9JMA9. Positions 35-598.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0733.
GeneTreeiENSGT00760000118857.
HOGENOMiHOG000116406.
HOVERGENiHBG071421.
InParanoidiQ9JMA9.
KOiK05038.
OMAiCINDTIN.
OrthoDBiEOG793B71.
PhylomeDBiQ9JMA9.
TreeFamiTF343812.

Family and domain databases

InterProiIPR000175. Na/ntran_symport.
[Graphical view]
PANTHERiPTHR11616. PTHR11616. 1 hit.
PfamiPF00209. SNF. 1 hit.
[Graphical view]
PRINTSiPR00176. NANEUSMPORT.
PROSITEiPS00610. NA_NEUROTRAN_SYMP_1. 1 hit.
PS00754. NA_NEUROTRAN_SYMP_2. 1 hit.
PS50267. NA_NEUROTRAN_SYMP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JMA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRLKCPNFF KCRQKEKVTA SSENFHVGEN DENQERGNWS KKSDYLLSMV
60 70 80 90 100
GYAVGLGNVW RFPYLTYTNG GGAFLIPYAI MLALAGLPLF FLECSLGQFA
110 120 130 140 150
SLGPVSVWRI LPLFQGVGIT MVLISVFVAI YYNVIIAYSL YYLFASFQSV
160 170 180 190 200
LPWANCSSWA DENCSRTPIV TGCNVSIGAG EMFMNISWVN TNNLTCLNGS
210 220 230 240 250
EVFRPGQLPS EQYWDKVTLQ RSSGMDETGV VVWYLALCLL LAWLIVGAAL
260 270 280 290 300
FKGIKSSGKV VYFTALFPYV VLLILLIRGA TLEGASKGIS YYIGAQSNFT
310 320 330 340 350
KLREAEVWKD AATQIFYSLS VAWGGLVALS SYNKFNNNCY SDAIIVCLTN
360 370 380 390 400
CLTSVFAGFA IFSILGHMAH ISGKEVSQVV KSGFDLAFIA YPEALAQLPA
410 420 430 440 450
GPFWSILFFF MLLTLGLDSQ FASIETITTT FQDLFPKAMK RMRVPITLGC
460 470 480 490 500
CLILFLLGLL CVTQAGIYWV HLIDHFCAGW GILIAAILEI AGIIWIYGGN
510 520 530 540 550
RFIEDIEMMI GAKRWIFWLW WRACWFVITP ILLSAILVWS LVKFHRPDYA
560 570 580 590 600
DIPYPDWGVA LGWCMIIFCI IWIPIMAIIK IVQAEGNILQ RIISCCRPAS
610 620 630
NWGPYLEKHR GERYRDMAEP AKETDHEIPT ISGSTKPE
Length:638
Mass (Da):71,456
Last modified:October 1, 2000 - v1
Checksum:i5D5A78E2DF7E7612
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901F → V in AAD49320 (Ref. 3) Curated
Sequence conflicti123 – 1231L → P in AAD49320 (Ref. 3) Curated
Sequence conflicti192 – 1921N → S in AAK43541 (PubMed:11306607).Curated
Sequence conflicti323 – 3231W → C in AAD49320 (Ref. 3) Curated
Sequence conflicti341 – 3411S → P in AAD49320 (Ref. 3) Curated
Sequence conflicti350 – 3501N → K in AAD49320 (Ref. 3) Curated
Sequence conflicti597 – 5971R → I in BAB31272 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033285 mRNA. Translation: BAA94300.1.
AF320226 mRNA. Translation: AAK43541.1.
AF161714 mRNA. Translation: AAD49320.1.
AK018553 mRNA. Translation: BAB31272.1.
CCDSiCCDS30051.1.
RefSeqiNP_064433.3. NM_020049.4.
UniGeneiMm.253984.

Genome annotation databases

EnsembliENSMUST00000033414; ENSMUSP00000033414; ENSMUSG00000031089.
GeneIDi56774.
KEGGimmu:56774.
UCSCiuc009sur.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033285 mRNA. Translation: BAA94300.1.
AF320226 mRNA. Translation: AAK43541.1.
AF161714 mRNA. Translation: AAD49320.1.
AK018553 mRNA. Translation: BAB31272.1.
CCDSiCCDS30051.1.
RefSeqiNP_064433.3. NM_020049.4.
UniGeneiMm.253984.

3D structure databases

ProteinModelPortaliQ9JMA9.
SMRiQ9JMA9. Positions 35-598.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033414.

PTM databases

PhosphoSiteiQ9JMA9.

Proteomic databases

PRIDEiQ9JMA9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033414; ENSMUSP00000033414; ENSMUSG00000031089.
GeneIDi56774.
KEGGimmu:56774.
UCSCiuc009sur.2. mouse.

Organism-specific databases

CTDi11254.
MGIiMGI:1890216. Slc6a14.

Phylogenomic databases

eggNOGiCOG0733.
GeneTreeiENSGT00760000118857.
HOGENOMiHOG000116406.
HOVERGENiHBG071421.
InParanoidiQ9JMA9.
KOiK05038.
OMAiCINDTIN.
OrthoDBiEOG793B71.
PhylomeDBiQ9JMA9.
TreeFamiTF343812.

Enzyme and pathway databases

ReactomeiREACT_301178. Amino acid transport across the plasma membrane.
REACT_307956. Na+/Cl- dependent neurotransmitter transporters.

Miscellaneous databases

NextBioi313306.
PROiQ9JMA9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JMA9.
ExpressionAtlasiQ9JMA9. baseline and differential.
GenevisibleiQ9JMA9. MM.

Family and domain databases

InterProiIPR000175. Na/ntran_symport.
[Graphical view]
PANTHERiPTHR11616. PTHR11616. 1 hit.
PfamiPF00209. SNF. 1 hit.
[Graphical view]
PRINTSiPR00176. NANEUSMPORT.
PROSITEiPS00610. NA_NEUROTRAN_SYMP_1. 1 hit.
PS00754. NA_NEUROTRAN_SYMP_2. 1 hit.
PS50267. NA_NEUROTRAN_SYMP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a mouse colonic system B(0+) amino acid transporter related to amino acid absorption in colon."
    Ugawa S., Sunouchi Y., Ueda T., Takahashi E., Saishin Y., Shimada S.
    Am. J. Physiol. 281:G365-G370(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: ddY.
  2. "Na(+)- and Cl(-)-coupled active transport of nitric oxide synthase inhibitors via amino acid transport system B(0,+)."
    Hatanaka T., Nakanishi T., Huang W., Leibach F.H., Prasad P.D., Ganapathy V., Ganapathy M.E.
    J. Clin. Invest. 107:1035-1043(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6.
    Tissue: Colon.
  3. Revell L., Sloan J.L., Mager S.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Lung.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon.

Entry informationi

Entry nameiS6A14_MOUSE
AccessioniPrimary (citable) accession number: Q9JMA9
Secondary accession number(s): Q91Y60, Q9D317, Q9R183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.