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Protein
Submitted name:

Antigen peptide transporter 1

Gene

Tap1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-bindingUniRule annotationImported, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Submitted name:
Antigen peptide transporter 1Imported
Submitted name:
Tap1 proteinImported
Submitted name:
Transporter 1, ATP-binding cassette, sub-family B (MDR/TAP)Imported
Gene namesi
Name:Tap1Imported
Synonyms:Arrb2-psImported, Hla-dmaImported, Hla-dmbImported, Psmb9Imported, RT1-BaImported, RT1-BbImported, RT1-DaImported, RT1-Db1Imported, RT1-Db2Imported, RT1-DObImported, tap1Imported, Tap2Imported, TesbImported
ORF Names:rCG_61064Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi3817. Tap1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei42 – 6221HelicalSequence analysisAdd
BLAST
Transmembranei69 – 9022HelicalSequence analysisAdd
BLAST
Transmembranei110 – 13122HelicalSequence analysisAdd
BLAST
Transmembranei164 – 18522HelicalSequence analysisAdd
BLAST
Transmembranei205 – 22622HelicalSequence analysisAdd
BLAST
Transmembranei291 – 31828HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 725699Sequence analysisPRO_5007206899Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000529.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini166 – 447282ABC transmembrane type-1InterPro annotationAdd
BLAST
Domaini480 – 719240ABC transporterInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ABC transporter domain.UniRule annotation

Keywords - Domaini

SignalSequence analysis, Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

eggNOGiKOG0058. Eukaryota.
COG1132. LUCA.
GeneTreeiENSGT00550000074497.
HOVERGENiHBG008358.
KOiK05653.
OMAiCLGEMAI.
OrthoDBiEOG7Z3F4H.
TreeFamiTF105197.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR013305. ABC_Tap-like.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
IPR013306. Tap1/ABCB2.
[Graphical view]
PANTHERiPTHR24221:SF249. PTHR24221:SF249. 2 hits.
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsiTIGR00958. 3a01208. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAHAWPTAA LLLLLVDWLL LRPVLPGIFS LLVPEVPLLR VWAVGLSRWA
60 70 80 90 100
ILGLGVRGVL GVTAGARGWL AALQPLVAAL GLALPGLASF RKLSAWGALR
110 120 130 140 150
EGDNAGLLHW NSRLDAFVLS YVAALPAAAL WHKLGGFWAP SGHKGAGDML
160 170 180 190 200
CRMLGFLDSK KGRLHLVLVL LILSCLGEMA IPFFTGRITD WILQDKTAPS
210 220 230 240 250
FARNMWLMCI LTVASTALEF AGDGIYNITM GHMHSRVHGE VFRAVLHQET
260 270 280 290 300
GFFLKNPTGS ITSRVTEDTS NVCESISDKL NLFLWYLGRG LCLLAFMIWG
310 320 330 340 350
SFYLTVVTLL SLPLLFLLPR RLGKVYQSLA VKVQESLAKS TQVALEALSA
360 370 380 390 400
MPTVRSFANE EGEAQKFRQK LEEMKPLNKK EALAYVTEVW TMSVSGMLLK
410 420 430 440 450
VGILYLGGQL VVRGAVSSGN LVSFVLYQLQ FTRAVEVLLS IYPSMQKSVG
460 470 480 490 500
ASEKIFEYLD RTPCSPLSGS LAPLNMKGLV KFQDVSFAYP NHPNVQVLQG
510 520 530 540 550
LTFTLYPGKV TALVGPNGSG KSTVAALLQN LYQPTGGKVL LDGELLVQYD
560 570 580 590 600
HHYLHTQVAA VGQEPLLFGR SFRENIAYGL TRTPTMEEIT AVAMESGAHD
610 620 630 640 650
FISGFPQGYD TEVGETGNQL SGGQRQAVAL ARALIRKPRL LILDDATSAL
660 670 680 690 700
DAGNQLRVQR LLYESPEWAS RTVLLITQQL SLAERAHHIL FLKEGSVCEQ
710 720
GTHLQLMERG GCYRSMVEAL AAPSD
Length:725
Mass (Da):79,124
Last modified:May 1, 1997 - v1
Checksum:i4481F5D1055410A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC098547 Genomic DNA. No translation available.
Y10230 mRNA. Translation: CAA71279.1.
Y10234 mRNA. Translation: CAA71283.1.
BX883043 Genomic DNA. Translation: CAE83941.1.
CH473988 Genomic DNA. Translation: EDL96810.1.
RefSeqiNP_114444.2. NM_032055.4.
UniGeneiRn.10763.

Genome annotation databases

EnsembliENSRNOT00000000529; ENSRNOP00000000529; ENSRNOG00000000457.
GeneIDi24811.
KEGGirno:24811.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC098547 Genomic DNA. No translation available.
Y10230 mRNA. Translation: CAA71279.1.
Y10234 mRNA. Translation: CAA71283.1.
BX883043 Genomic DNA. Translation: CAE83941.1.
CH473988 Genomic DNA. Translation: EDL96810.1.
RefSeqiNP_114444.2. NM_032055.4.
UniGeneiRn.10763.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000529.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000529; ENSRNOP00000000529; ENSRNOG00000000457.
GeneIDi24811.
KEGGirno:24811.

Organism-specific databases

CTDi6890.
RGDi3817. Tap1.

Phylogenomic databases

eggNOGiKOG0058. Eukaryota.
COG1132. LUCA.
GeneTreeiENSGT00550000074497.
HOVERGENiHBG008358.
KOiK05653.
OMAiCLGEMAI.
OrthoDBiEOG7Z3F4H.
TreeFamiTF105197.

Enzyme and pathway databases

ReactomeiR-RNO-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

NextBioi604494.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR013305. ABC_Tap-like.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
IPR013306. Tap1/ABCB2.
[Graphical view]
PANTHERiPTHR24221:SF249. PTHR24221:SF249. 2 hits.
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsiTIGR00958. 3a01208. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Deverson E.V.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported and PVGImported.
    Tissue: Activated lymphocytesImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Brown NorwayImported.
  3. "The genomic sequence and comparative analysis of the rat major histocompatibility complex."
    Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.
    Genome Res. 14:631-639(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Brown NorwayImported.
  4. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  6. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  7. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiP97949_RAT
AccessioniPrimary (citable) accession number: P97949
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.