ID   B6VNV2_HUMAN            Unreviewed;       209 AA.
AC   B6VNV2;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Truncated antigen peptide transporter 2 {ECO:0000313|EMBL:CAR92541.1};
GN   Name=TAP2 {ECO:0000313|EMBL:CAR92541.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:CAR92541.1};
RN   [1] {ECO:0000313|EMBL:CAR92541.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gonzalez-Santesteban C.P., Espana A., de la Calle-Martin O.;
RT   "A novel mutation in the TAP2 gene in bare lymphocyte syndrome leading to
RT   metastatic squamous cell carcinoma of skin.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAR92541.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gonzalez-Santesteban C.P.;
RT   "Molecular analysis of the mutant CD8 glycoprotein responsible for familial
RT   CD8 deficiency.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAR92541.1}
RP   NUCLEOTIDE SEQUENCE.
RA   De La Calle-Martin O.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FM246456; CAR92541.1; -; mRNA.
DR   AlphaFoldDB; B6VNV2; -.
DR   PeptideAtlas; B6VNV2; -.
DR   GO; GO:0042825; C:TAP complex; IEA:InterPro.
DR   GO; GO:0015440; F:ABC-type peptide transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0042287; F:MHC protein binding; IEA:InterPro.
DR   GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR005293; Tap2/ABCB3.
DR   PRINTS; PR01897; TAP2PROTEIN.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        58..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   209 AA;  22450 MW;  F673ECE5F1C10127 CRC64;
     MRLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGLPGLWL EGTLRLGGLW GLLKLRGLLG
     FVGTLLLPLC LATPLTVSLR ALVAGASRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS
     PPGAQEKEQD QVNNKVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP HYSGRVIDIL
     GGDFDPHAFA SAIFFMCLFS FGSSLSAGC
//