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Q9JMA9 (S6A14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Slc6a14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na+/Cl--dependent manner. Ref.1 Ref.2

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in the distal region of the intestinal tract: cecum and colon. Ref.1 Ref.2

Sequence similarities

Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A14 subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 638638Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+)
PRO_0000214796

Regions

Topological domain1 – 4444Cytoplasmic Potential
Transmembrane45 – 6521Helical; Name=1; Potential
Transmembrane72 – 9221Helical; Name=2; Potential
Transmembrane110 – 13021Helical; Name=3; Potential
Topological domain131 – 230100Extracellular Potential
Transmembrane231 – 25121Helical; Name=4; Potential
Transmembrane257 – 27721Helical; Name=5; Potential
Transmembrane311 – 33121Helical; Name=6; Potential
Transmembrane344 – 36421Helical; Name=7; Potential
Transmembrane395 – 41521Helical; Name=8; Potential
Transmembrane453 – 47321Helical; Name=9; Potential
Transmembrane476 – 49621Helical; Name=10; Potential
Transmembrane524 – 54421Helical; Name=11; Potential
Transmembrane559 – 57921Helical; Name=12; Potential
Topological domain580 – 63859Cytoplasmic Potential

Amino acid modifications

Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict901F → V in AAD49320. Ref.3
Sequence conflict1231L → P in AAD49320. Ref.3
Sequence conflict1921N → S in AAK43541. Ref.2
Sequence conflict3231W → C in AAD49320. Ref.3
Sequence conflict3411S → P in AAD49320. Ref.3
Sequence conflict3501N → K in AAD49320. Ref.3
Sequence conflict5971R → I in BAB31272. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9JMA9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5D5A78E2DF7E7612

FASTA63871,456
        10         20         30         40         50         60 
MDRLKCPNFF KCRQKEKVTA SSENFHVGEN DENQERGNWS KKSDYLLSMV GYAVGLGNVW 

        70         80         90        100        110        120 
RFPYLTYTNG GGAFLIPYAI MLALAGLPLF FLECSLGQFA SLGPVSVWRI LPLFQGVGIT 

       130        140        150        160        170        180 
MVLISVFVAI YYNVIIAYSL YYLFASFQSV LPWANCSSWA DENCSRTPIV TGCNVSIGAG 

       190        200        210        220        230        240 
EMFMNISWVN TNNLTCLNGS EVFRPGQLPS EQYWDKVTLQ RSSGMDETGV VVWYLALCLL 

       250        260        270        280        290        300 
LAWLIVGAAL FKGIKSSGKV VYFTALFPYV VLLILLIRGA TLEGASKGIS YYIGAQSNFT 

       310        320        330        340        350        360 
KLREAEVWKD AATQIFYSLS VAWGGLVALS SYNKFNNNCY SDAIIVCLTN CLTSVFAGFA 

       370        380        390        400        410        420 
IFSILGHMAH ISGKEVSQVV KSGFDLAFIA YPEALAQLPA GPFWSILFFF MLLTLGLDSQ 

       430        440        450        460        470        480 
FASIETITTT FQDLFPKAMK RMRVPITLGC CLILFLLGLL CVTQAGIYWV HLIDHFCAGW 

       490        500        510        520        530        540 
GILIAAILEI AGIIWIYGGN RFIEDIEMMI GAKRWIFWLW WRACWFVITP ILLSAILVWS 

       550        560        570        580        590        600 
LVKFHRPDYA DIPYPDWGVA LGWCMIIFCI IWIPIMAIIK IVQAEGNILQ RIISCCRPAS 

       610        620        630 
NWGPYLEKHR GERYRDMAEP AKETDHEIPT ISGSTKPE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB033285 mRNA. Translation: BAA94300.1.
AF320226 mRNA. Translation: AAK43541.1.
AF161714 mRNA. Translation: AAD49320.1.
AK018553 mRNA. Translation: BAB31272.1.
RefSeqNP_064433.3. NM_020049.4.
UniGeneMm.253984.

3D structure databases

ProteinModelPortalQ9JMA9.
SMRQ9JMA9. Positions 35-598.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9JMA9.

Proteomic databases

PRIDEQ9JMA9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033414; ENSMUSP00000033414; ENSMUSG00000031089.
GeneID56774.
KEGGmmu:56774.
UCSCuc009sur.2. mouse.

Organism-specific databases

CTD11254.
MGIMGI:1890216. Slc6a14.

Phylogenomic databases

eggNOGCOG0733.
GeneTreeENSGT00740000115427.
HOGENOMHOG000116406.
HOVERGENHBG071421.
InParanoidQ9JMA9.
KOK05038.
OMASSGMNET.
OrthoDBEOG793B71.
PhylomeDBQ9JMA9.
TreeFamTF343812.

Gene expression databases

ArrayExpressQ9JMA9.
BgeeQ9JMA9.
GenevestigatorQ9JMA9.

Family and domain databases

InterProIPR000175. Na/ntran_symport.
[Graphical view]
PANTHERPTHR11616. PTHR11616. 1 hit.
PfamPF00209. SNF. 1 hit.
[Graphical view]
PRINTSPR00176. NANEUSMPORT.
PROSITEPS00610. NA_NEUROTRAN_SYMP_1. 1 hit.
PS00754. NA_NEUROTRAN_SYMP_2. 1 hit.
PS50267. NA_NEUROTRAN_SYMP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio313306.
PROQ9JMA9.
SOURCESearch...

Entry information

Entry nameS6A14_MOUSE
AccessionPrimary (citable) accession number: Q9JMA9
Secondary accession number(s): Q91Y60, Q9D317, Q9R183
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot