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P21958

- TAP1_MOUSE

UniProt

P21958 - TAP1_MOUSE

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Protein

Antigen peptide transporter 1

Gene

Tap1

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

Functioni

Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi514 – 5218ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ADP binding Source: Ensembl
  2. ATPase activity, coupled to transmembrane movement of substances Source: RefGenome
  3. ATP binding Source: UniProtKB-KW
  4. MHC class I protein binding Source: MGI
  5. peptide transporter activity Source: InterPro

GO - Biological processi

  1. antigen processing and presentation of endogenous peptide antigen via MHC class I Source: Ensembl
  2. cytosol to ER transport Source: Ensembl
  3. defense response Source: MGI
  4. intracellular transport of viral protein in host cell Source: Ensembl
  5. transmembrane transport Source: RefGenome
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity, Peptide transport, Protein transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_199105. ER-Phagosome pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Antigen peptide transporter 1
Short name:
APT1
Alternative name(s):
ATP-binding cassette sub-family B member 2
Histocompatibility antigen modifier 1
Peptide transporter TAP1
Gene namesi
Name:Tap1
Synonyms:Abcb2, Ham-1, Ham1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:98483. Tap1.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein
Note: The transmembrane segments seem to form a pore in the membrane.

GO - Cellular componenti

  1. integral component of membrane Source: RefGenome
  2. mitochondrion Source: MGI
  3. phagocytic vesicle membrane Source: Reactome
  4. TAP complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724Antigen peptide transporter 1PRO_0000093327Add
BLAST

Proteomic databases

MaxQBiP21958.
PaxDbiP21958.
PRIDEiP21958.

PTM databases

PhosphoSiteiP21958.

Expressioni

Gene expression databases

BgeeiP21958.
ExpressionAtlasiP21958. baseline and differential.
GenevestigatoriP21958.

Interactioni

Subunit structurei

Heterodimer of TAP1 and TAP2. Interacts with PSMB5 and PSMB8 (By similarity).By similarity

Protein-protein interaction databases

BioGridi203966. 1 interaction.
IntActiP21958. 2 interactions.
MINTiMINT-4136864.

Structurei

3D structure databases

ProteinModelPortaliP21958.
SMRiP21958. Positions 151-718.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini33 – 364LumenalSequence Analysis
Topological domaini60 – 689CytoplasmicSequence Analysis
Topological domaini90 – 10920LumenalSequence AnalysisAdd
BLAST
Topological domaini131 – 16232CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini184 – 20320LumenalSequence AnalysisAdd
BLAST
Topological domaini225 – 27450CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini296 – 3049LumenalSequence Analysis
Topological domaini326 – 39469CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini416 – 4194LumenalSequence Analysis
Topological domaini441 – 724284CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221Helical; Name=1PROSITE-ProRule annotationAdd
BLAST
Transmembranei37 – 5923Helical; Name=2PROSITE-ProRule annotationAdd
BLAST
Transmembranei69 – 8921Helical; Name=3PROSITE-ProRule annotationAdd
BLAST
Transmembranei110 – 13021Helical; Name=4PROSITE-ProRule annotationAdd
BLAST
Transmembranei163 – 18321Helical; Name=5PROSITE-ProRule annotationAdd
BLAST
Transmembranei204 – 22421Helical; Name=6PROSITE-ProRule annotationAdd
BLAST
Transmembranei275 – 29521Helical; Name=7PROSITE-ProRule annotationAdd
BLAST
Transmembranei305 – 32521Helical; Name=8PROSITE-ProRule annotationAdd
BLAST
Transmembranei395 – 41521Helical; Name=9PROSITE-ProRule annotationAdd
BLAST
Transmembranei420 – 44021Helical; Name=10PROSITE-ProRule annotationAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 446284ABC transmembrane type-1PROSITE-ProRule annotationAdd
BLAST
Domaini479 – 718240ABC transporterPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni351 – 39646Involved in peptide-binding siteBy similarityAdd
BLAST
Regioni429 – 46335Involved in peptide-binding siteBy similarityAdd
BLAST

Domaini

The peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2.By similarity

Sequence similaritiesi

Contains 1 ABC transmembrane type-1 domain.PROSITE-ProRule annotation
Contains 1 ABC transporter domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1132.
GeneTreeiENSGT00550000074497.
HOVERGENiHBG008358.
InParanoidiP21958.
KOiK05653.
OMAiCLGSEIR.
OrthoDBiEOG7Z3F4H.
PhylomeDBiP21958.
TreeFamiTF105197.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR013305. ABC_B2.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR005293. Ag_transporter2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
PRINTSiPR01896. TAP1PROTEIN.
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.

P21958-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAHVWLAAA LLLLVDWLLL RPMLPGIFSL LVPEVPLLRV WVVGLSRWAI
60 70 80 90 100
LGLGVRGVLG VTAGAHGWLA ALQPLVAALS LALPGLALFR ELAAWGTLRE
110 120 130 140 150
GDSAGLLYWN SRPDAFAISY VAALPAAALW HKLGSLWAPS GNRDAGDMLC
160 170 180 190 200
RMLGFLGPKK RRLYLVLVLL ILSCLGEMAI PFFTGRITDW ILQDKTVPSF
210 220 230 240 250
TRNIWLMSIL TIASTALEFA SDGIYNITMG HMHGRVHREV FRAVLRQETG
260 270 280 290 300
FFLKNPAGSI TSRVTEDTAN VCESISGTLS LLLWYLGRAL CLLVFMFWGS
310 320 330 340 350
PYLTLVTLIN LPLLFLLPKK LGKVHQSLAV KVQESLAKST QVALEALSAM
360 370 380 390 400
PTVRSFANEE GEAQKFRQKL EEMKTLNKKE ALAYVAEVWT TSVSGMLLKV
410 420 430 440 450
GILYLGGQLV IRGAVSSGNL VSFVLYQLQF TQAVQVLLSL YPSMQKAVGS
460 470 480 490 500
SEKIFEYLDR TPCSPLSGSL APSNMKGLVE FQDVSFAYPN QPKVQVLQGL
510 520 530 540 550
TFTLHPGTVT ALVGPNGSGK STVAALLQNL YQPTGGQLLL DGQCLVQYDH
560 570 580 590 600
HYLHTQVAAV GQEPLLFGRS FRENIAYGLN RTPTMEEITA VAVESGAHDF
610 620 630 640 650
ISGFPQGYDT EVGETGNQLS GGQRQAVALA RALIRKPLLL ILDDATSALD
660 670 680 690 700
AGNQLRVQRL LYESPKRASR TVLLITQQLS LAEQAHHILF LREGSVGEQG
710 720
THLQLMKRGG CYRAMVEALA APAD
Length:724
Mass (Da):78,864
Last modified:June 28, 2011 - v3
Checksum:iA08E40F9F5FBAE9D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771G → D in AAB41962. (PubMed:9164943)Curated
Sequence conflicti277 – 2771G → D in AAA39570. (PubMed:2270487)Curated
Sequence conflicti277 – 2771G → D in CAA42178. 1 PublicationCurated
Sequence conflicti355 – 3551S → Q in CAA42178. 1 PublicationCurated
Sequence conflicti414 – 4141A → T in AAB41962. (PubMed:9164943)Curated
Sequence conflicti414 – 4141A → T in AAA39570. (PubMed:2270487)Curated
Sequence conflicti414 – 4141A → T in CAA42178. 1 PublicationCurated
Sequence conflicti481 – 4811F → L in CAA42178. 1 PublicationCurated
Sequence conflicti544 – 5441C → R in AAB41962. (PubMed:9164943)Curated
Sequence conflicti544 – 5441C → R in AAA39570. (PubMed:2270487)Curated
Sequence conflicti544 – 5441C → R in CAA42178. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U60018 mRNA. Translation: AAB41962.1.
U60019 mRNA. Translation: AAB41963.1.
AK162731 mRNA. Translation: BAE37041.1.
AF027865 Genomic DNA. Translation: AAB81534.1.
CH466660 Genomic DNA. Translation: EDL10260.1.
M55637 mRNA. Translation: AAA39570.1.
X59615 mRNA. Translation: CAA42178.1.
CCDSiCCDS28643.1.
PIRiA37779.
JC2020.
RefSeqiNP_038711.2. NM_013683.2.
UniGeneiMm.482076.

Genome annotation databases

EnsembliENSMUST00000170086; ENSMUSP00000128401; ENSMUSG00000037321.
GeneIDi21354.
KEGGimmu:21354.
UCSCiuc008cbu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U60018 mRNA. Translation: AAB41962.1 .
U60019 mRNA. Translation: AAB41963.1 .
AK162731 mRNA. Translation: BAE37041.1 .
AF027865 Genomic DNA. Translation: AAB81534.1 .
CH466660 Genomic DNA. Translation: EDL10260.1 .
M55637 mRNA. Translation: AAA39570.1 .
X59615 mRNA. Translation: CAA42178.1 .
CCDSi CCDS28643.1.
PIRi A37779.
JC2020.
RefSeqi NP_038711.2. NM_013683.2.
UniGenei Mm.482076.

3D structure databases

ProteinModelPortali P21958.
SMRi P21958. Positions 151-718.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203966. 1 interaction.
IntActi P21958. 2 interactions.
MINTi MINT-4136864.

PTM databases

PhosphoSitei P21958.

Proteomic databases

MaxQBi P21958.
PaxDbi P21958.
PRIDEi P21958.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000170086 ; ENSMUSP00000128401 ; ENSMUSG00000037321 .
GeneIDi 21354.
KEGGi mmu:21354.
UCSCi uc008cbu.2. mouse.

Organism-specific databases

CTDi 6890.
MGIi MGI:98483. Tap1.

Phylogenomic databases

eggNOGi COG1132.
GeneTreei ENSGT00550000074497.
HOVERGENi HBG008358.
InParanoidi P21958.
KOi K05653.
OMAi CLGSEIR.
OrthoDBi EOG7Z3F4H.
PhylomeDBi P21958.
TreeFami TF105197.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_199105. ER-Phagosome pathway.

Miscellaneous databases

NextBioi 300552.
PROi P21958.
SOURCEi Search...

Gene expression databases

Bgeei P21958.
ExpressionAtlasi P21958. baseline and differential.
Genevestigatori P21958.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR013305. ABC_B2.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR005293. Ag_transporter2.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view ]
PRINTSi PR01896. TAP1PROTEIN.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsi TIGR00958. 3a01208. 1 hit.
PROSITEi PS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Allelic variation in the mouse Tap-1 and Tap-2 transporter genes."
    Marusina K., Iyer M., Monaco J.J.
    J. Immunol. 158:5251-5256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: WEHI-3.
    Tissue: T-cell lymphoma.
  2. "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: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Transport protein genes in the murine MHC: possible implications for antigen processing."
    Monaco J.J., Cho S., Attaya M.
    Science 250:1723-1726(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 148-724.
  6. Sun X.Y., Zhou J., Frazer I.
    Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 148-724.
    Strain: BALB/c.

Entry informationi

Entry nameiTAP1_MOUSE
AccessioniPrimary (citable) accession number: P21958
Secondary accession number(s): Q62427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 28, 2011
Last modified: October 29, 2014
This is version 145 of the entry and version 3 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