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Protein

Solute carrier family 2, facilitated glucose transporter member 12

Gene

SLC2A12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Facilitative glucose transporter.By similarity

GO - Molecular functioni

  1. substrate-specific transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. glucose transport Source: Ensembl
  2. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

ReactomeiREACT_19343. Facilitative Na+-independent glucose transporters.

Protein family/group databases

TCDBi2.A.1.1.87. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 2, facilitated glucose transporter member 12
Alternative name(s):
Glucose transporter type 12
Short name:
GLUT-12
Gene namesi
Name:SLC2A12
Synonyms:GLUT12, GLUT8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:18067. SLC2A12.

Subcellular locationi

Endomembrane system By similarity; Multi-pass membrane protein By similarity. Cytoplasmperinuclear region 1 Publication
Note: Localizes primarily perinuclear region in the absence of insulin.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei45 – 6521HelicalSequence AnalysisAdd
BLAST
Topological domaini66 – 8015ExtracellularSequence AnalysisAdd
BLAST
Transmembranei81 – 10121HelicalSequence AnalysisAdd
BLAST
Topological domaini102 – 11514CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei116 – 13621HelicalSequence AnalysisAdd
BLAST
Topological domaini137 – 1371ExtracellularSequence Analysis
Transmembranei138 – 15821HelicalSequence AnalysisAdd
BLAST
Topological domaini159 – 17214CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence AnalysisAdd
BLAST
Topological domaini194 – 1974ExtracellularSequence Analysis
Transmembranei198 – 21821HelicalSequence AnalysisAdd
BLAST
Topological domaini219 – 27860CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei279 – 29921HelicalSequence AnalysisAdd
BLAST
Topological domaini300 – 31718ExtracellularSequence AnalysisAdd
BLAST
Transmembranei318 – 33821HelicalSequence AnalysisAdd
BLAST
Topological domaini339 – 3457CytoplasmicSequence Analysis
Transmembranei346 – 36621HelicalSequence AnalysisAdd
BLAST
Topological domaini367 – 466100ExtracellularSequence AnalysisAdd
BLAST
Transmembranei467 – 48721HelicalSequence AnalysisAdd
BLAST
Topological domaini488 – 49811CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei499 – 51921HelicalSequence AnalysisAdd
BLAST
Topological domaini520 – 5289ExtracellularSequence Analysis
Transmembranei529 – 54921HelicalSequence AnalysisAdd
BLAST
Topological domaini550 – 61768CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endomembrane system Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617Solute carrier family 2, facilitated glucose transporter member 12PRO_0000292014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi383 – 3831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8TD20.
PRIDEiQ8TD20.

PTM databases

PhosphoSiteiQ8TD20.

Expressioni

Tissue specificityi

Predominantly expressed in skeletal muscle, heart and prostate, with lower levels in brain, placenta and kidney.1 Publication

Gene expression databases

BgeeiQ8TD20.
CleanExiHS_SLC2A12.
GenevestigatoriQ8TD20.

Organism-specific databases

HPAiHPA031593.

Interactioni

Protein-protein interaction databases

BioGridi127535. 2 interactions.
STRINGi9606.ENSP00000275230.

Structurei

3D structure databases

ProteinModelPortaliQ8TD20.
SMRiQ8TD20. Positions 59-364, 463-560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00590000083062.
HOGENOMiHOG000202868.
HOVERGENiHBG051858.
InParanoidiQ8TD20.
KOiK08149.
OMAiNFAITVS.
OrthoDBiEOG75B852.
PhylomeDBiQ8TD20.
TreeFamiTF332408.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 2 hits.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 2 hits.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8TD20-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVPVENTEGP SLLNQKGTAV ETEGSGSRHP PWARGCGMFT FLSSVTAAVS
60 70 80 90 100
GLLVGYELGI ISGALLQIKT LLALSCHEQE MVVSSLVIGA LLASLTGGVL
110 120 130 140 150
IDRYGRRTAI ILSSCLLGLG SLVLILSLSY TVLIVGRIAI GVSISLSSIA
160 170 180 190 200
TCVYIAEIAP QHRRGLLVSL NELMIVIGIL SAYISNYAFA NVFHGWKYMF
210 220 230 240 250
GLVIPLGVLQ AIAMYFLPPS PRFLVMKGQE GAASKVLGRL RALSDTTEEL
260 270 280 290 300
TVIKSSLKDE YQYSFWDLFR SKDNMRTRIM IGLTLVFFVQ ITGQPNILFY
310 320 330 340 350
ASTVLKSVGF QSNEAASLAS TGVGVVKVIS TIPATLLVDH VGSKTFLCIG
360 370 380 390 400
SSVMAASLVT MGIVNLNIHM NFTHICRSHN SINQSLDESV IYGPGNLSTN
410 420 430 440 450
NNTLRDHFKG ISSHSRSSLM PLRNDVDKRG ETTSASLLNA GLSHTEYQIV
460 470 480 490 500
TDPGDVPAFL KWLSLASLLV YVAAFSIGLG PMPWLVLSEI FPGGIRGRAM
510 520 530 540 550
ALTSSMNWGI NLLISLTFLT VTDLIGLPWV CFIYTIMSLA SLLFVVMFIP
560 570 580 590 600
ETKGCSLEQI SMELAKVNYV KNNICFMSHH QEELVPKQPQ KRKPQEQLLE
610
CNKLCGRGQS RQLSPET
Length:617
Mass (Da):66,966
Last modified:June 1, 2002 - v1
Checksum:iF176325CDED15249
GO

Sequence cautioni

The sequence BAB71214.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046419 mRNA. Translation: AAL02327.1.
AK056554 mRNA. Translation: BAB71214.1. Different initiation.
AK122628 mRNA. Translation: BAG53629.1.
AL035699, AL449363 Genomic DNA. Translation: CAD92514.2.
AL449363, AL035699 Genomic DNA. Translation: CAI17977.1.
CH471051 Genomic DNA. Translation: EAW47994.1.
BC070149 mRNA. Translation: AAH70149.1.
CCDSiCCDS5169.1.
RefSeqiNP_660159.1. NM_145176.2.
UniGeneiHs.486508.

Genome annotation databases

EnsembliENST00000275230; ENSP00000275230; ENSG00000146411.
GeneIDi154091.
KEGGihsa:154091.
UCSCiuc003qem.1. human.

Polymorphism databases

DMDMi74762615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046419 mRNA. Translation: AAL02327.1.
AK056554 mRNA. Translation: BAB71214.1. Different initiation.
AK122628 mRNA. Translation: BAG53629.1.
AL035699, AL449363 Genomic DNA. Translation: CAD92514.2.
AL449363, AL035699 Genomic DNA. Translation: CAI17977.1.
CH471051 Genomic DNA. Translation: EAW47994.1.
BC070149 mRNA. Translation: AAH70149.1.
CCDSiCCDS5169.1.
RefSeqiNP_660159.1. NM_145176.2.
UniGeneiHs.486508.

3D structure databases

ProteinModelPortaliQ8TD20.
SMRiQ8TD20. Positions 59-364, 463-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127535. 2 interactions.
STRINGi9606.ENSP00000275230.

Protein family/group databases

TCDBi2.A.1.1.87. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteiQ8TD20.

Polymorphism databases

DMDMi74762615.

Proteomic databases

PaxDbiQ8TD20.
PRIDEiQ8TD20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275230; ENSP00000275230; ENSG00000146411.
GeneIDi154091.
KEGGihsa:154091.
UCSCiuc003qem.1. human.

Organism-specific databases

CTDi154091.
GeneCardsiGC06M134349.
H-InvDBHIX0006232.
HGNCiHGNC:18067. SLC2A12.
HPAiHPA031593.
MIMi610372. gene.
neXtProtiNX_Q8TD20.
PharmGKBiPA38288.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00590000083062.
HOGENOMiHOG000202868.
HOVERGENiHBG051858.
InParanoidiQ8TD20.
KOiK08149.
OMAiNFAITVS.
OrthoDBiEOG75B852.
PhylomeDBiQ8TD20.
TreeFamiTF332408.

Enzyme and pathway databases

ReactomeiREACT_19343. Facilitative Na+-independent glucose transporters.

Miscellaneous databases

ChiTaRSiSLC2A12. human.
GeneWikiiSLC2A12.
GenomeRNAii154091.
NextBioi87232.
PROiQ8TD20.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TD20.
CleanExiHS_SLC2A12.
GenevestigatoriQ8TD20.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 2 hits.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 2 hits.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel glucose transporter-like protein -- GLUT-12."
    Rogers S., Macheda M.L., Docherty S.E., Carty M.D., Henderson M.A., Soeller W.C., Gibbs E.M., James D.E., Best J.D.
    Am. J. Physiol. 282:E733-E738(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Meninges and Skin.

Entry informationi

Entry nameiGTR12_HUMAN
AccessioniPrimary (citable) accession number: Q8TD20
Secondary accession number(s): B3KV17, Q7Z6U3, Q96MR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 1, 2002
Last modified: January 7, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.