TPSNR_HUMAN
ID TPSNR_HUMAN Reviewed; 468 AA.
AC Q9BX59; Q9NWB8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Tapasin-related protein;
DE Short=TAPASIN-R;
DE AltName: Full=TAP-binding protein-like;
DE AltName: Full=TAP-binding protein-related protein;
DE Short=TAPBP-R;
DE AltName: Full=Tapasin-like;
DE Flags: Precursor;
GN Name=TAPBPL;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), SUBCELLULAR LOCATION, AND
RP VARIANTS ARG-151 AND MET-334.
RX PubMed=11920573;
RX DOI=10.1002/1521-4141(200204)32:4<1059::aid-immu1059>3.0.co;2-g;
RA Teng M.S., Stephens R., Du Pasquier L., Freeman T., Lindquist J.A.,
RA Trowsdale J.;
RT "A human TAPBP (TAPASIN)-related gene, TAPBP-R.";
RL Eur. J. Immunol. 32:1059-1068(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANTS
RP VAL-42; VAL-146; ARG-151; ALA-165 AND VAL-169.
RC TISSUE=Embryo, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANTS
RP VAL-42; VAL-146; ALA-165 AND VAL-169.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 19-33.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [6]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23401559; DOI=10.1073/pnas.1222342110;
RA Boyle L.H., Hermann C., Boname J.M., Porter K.M., Patel P.A., Burr M.L.,
RA Duncan L.M., Harbour M.E., Rhodes D.A., Skjodt K., Lehner P.J.,
RA Trowsdale J.;
RT "Tapasin-related protein TAPBPR is an additional component of the MHC class
RT I presentation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3465-3470(2013).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS ALPHA; BETA; GAMMA; DELTA; EPSILON; ETA AND
RP ZETA).
RX PubMed=24444341; DOI=10.1111/imm.12253;
RA Porter K.M., Hermann C., Traherne J.A., Boyle L.H.;
RT "TAPBPR isoforms exhibit altered association with MHC class I.";
RL Immunology 142:289-299(2014).
RN [8]
RP FUNCTION, AND INTERACTION WITH HLA-A*02-B2M.
RX PubMed=26869717; DOI=10.1073/pnas.1519894113;
RA Morozov G.I., Zhao H., Mage M.G., Boyd L.F., Jiang J., Dolan M.A.,
RA Venna R., Norcross M.A., McMurtrey C.P., Hildebrand W., Schuck P.,
RA Natarajan K., Margulies D.H.;
RT "Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes
RT peptide editing.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1006-E1015(2016).
CC -!- FUNCTION: Component of the antigen processing and presentation pathway,
CC which binds to MHC class I coupled with beta2-microglobulin/B2M.
CC Association between TAPBPR and MHC class I occurs in the absence of a
CC functional peptide-loading complex (PLC). {ECO:0000269|PubMed:23401559,
CC ECO:0000269|PubMed:26869717}.
CC -!- SUBUNIT: Interacts with peptide-free HLA-A*02-B2M complexes or those
CC loaded with low affinity peptides, likely facilitating peptide exchange
CC onto higher affinity peptides. {ECO:0000269|PubMed:26869717}.
CC -!- INTERACTION:
CC Q9BX59; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12017416, EBI-3867333;
CC Q9BX59; P01892: HLA-A; NbExp=17; IntAct=EBI-12017416, EBI-2839473;
CC Q9BX59; P01889: HLA-B; NbExp=3; IntAct=EBI-12017416, EBI-1046513;
CC Q9BX59; Q15323: KRT31; NbExp=3; IntAct=EBI-12017416, EBI-948001;
CC Q9BX59; O76011: KRT34; NbExp=3; IntAct=EBI-12017416, EBI-1047093;
CC Q9BX59; Q92764: KRT35; NbExp=3; IntAct=EBI-12017416, EBI-1058674;
CC Q9BX59; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12017416, EBI-10171774;
CC Q9BX59; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12017416, EBI-22310682;
CC Q9BX59; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-12017416, EBI-11339910;
CC Q9BX59; P15884-3: TCF4; NbExp=3; IntAct=EBI-12017416, EBI-13636688;
CC Q9BX59; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-12017416, EBI-11139477;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11920573};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:11920573}.
CC Endoplasmic reticulum membrane {ECO:0000305|PubMed:11920573}; Single-
CC pass type I membrane protein {ECO:0000305|PubMed:11920573}. Microsome
CC membrane {ECO:0000305|PubMed:11920573}; Single-pass type I membrane
CC protein {ECO:0000305|PubMed:11920573}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:23401559}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:23401559}. Note=Mainly found in endoplasmic
CC reticulum but a minority is found on the cell surface
CC (PubMed:11920573).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=alpha;
CC IsoId=Q9BX59-1; Sequence=Displayed;
CC Name=beta;
CC IsoId=Q9BX59-2; Sequence=VSP_057096;
CC Name=gamma;
CC IsoId=Q9BX59-3; Sequence=VSP_057094;
CC Name=delta;
CC IsoId=Q9BX59-4; Sequence=VSP_057091, VSP_057092;
CC Name=epsilon;
CC IsoId=Q9BX59-5; Sequence=VSP_057089;
CC Name=eta;
CC IsoId=Q9BX59-6; Sequence=VSP_057090, VSP_057093;
CC Name=zeta;
CC IsoId=Q9BX59-7; Sequence=VSP_057095;
CC -!- INDUCTION: By interferon gamma. {ECO:0000269|PubMed:23401559}.
CC -!- MISCELLANEOUS: [Isoform beta]: Has reduced cell surface expression, and
CC does not down-regulate MHC class I surface expression as efficiently as
CC isoform alpha. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform gamma]: Does not interact with MHC class I.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform delta]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
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DR EMBL; AK001005; BAA91465.1; -; mRNA.
DR EMBL; AK002056; BAB41077.1; -; mRNA.
DR EMBL; AC005840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015017; AAH15017.1; -; mRNA.
DR CCDS; CCDS8546.1; -. [Q9BX59-1]
DR RefSeq; NP_060479.3; NM_018009.4. [Q9BX59-1]
DR PDB; 5WER; X-ray; 3.41 A; C/F/I/L=22-410.
DR PDBsum; 5WER; -.
DR AlphaFoldDB; Q9BX59; -.
DR SMR; Q9BX59; -.
DR BioGRID; 120395; 13.
DR IntAct; Q9BX59; 12.
DR STRING; 9606.ENSP00000266556; -.
DR iPTMnet; Q9BX59; -.
DR PhosphoSitePlus; Q9BX59; -.
DR BioMuta; TAPBPL; -.
DR DMDM; 296452847; -.
DR EPD; Q9BX59; -.
DR jPOST; Q9BX59; -.
DR MassIVE; Q9BX59; -.
DR MaxQB; Q9BX59; -.
DR PaxDb; Q9BX59; -.
DR PeptideAtlas; Q9BX59; -.
DR PRIDE; Q9BX59; -.
DR ProteomicsDB; 79351; -. [Q9BX59-1]
DR Antibodypedia; 22408; 352 antibodies from 23 providers.
DR DNASU; 55080; -.
DR Ensembl; ENST00000266556.8; ENSP00000266556.7; ENSG00000139192.12. [Q9BX59-1]
DR GeneID; 55080; -.
DR KEGG; hsa:55080; -.
DR MANE-Select; ENST00000266556.8; ENSP00000266556.7; NM_018009.5; NP_060479.3.
DR UCSC; uc001qog.5; human. [Q9BX59-1]
DR CTD; 55080; -.
DR DisGeNET; 55080; -.
DR GeneCards; TAPBPL; -.
DR HGNC; HGNC:30683; TAPBPL.
DR HPA; ENSG00000139192; Low tissue specificity.
DR MalaCards; TAPBPL; -.
DR MIM; 607081; gene.
DR neXtProt; NX_Q9BX59; -.
DR OpenTargets; ENSG00000139192; -.
DR PharmGKB; PA134955671; -.
DR VEuPathDB; HostDB:ENSG00000139192; -.
DR eggNOG; ENOG502QSXA; Eukaryota.
DR GeneTree; ENSGT00940000160453; -.
DR HOGENOM; CLU_033813_0_0_1; -.
DR InParanoid; Q9BX59; -.
DR OMA; DVVVTWI; -.
DR OrthoDB; 1369855at2759; -.
DR PhylomeDB; Q9BX59; -.
DR TreeFam; TF334274; -.
DR PathwayCommons; Q9BX59; -.
DR SignaLink; Q9BX59; -.
DR BioGRID-ORCS; 55080; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; TAPBPL; human.
DR GenomeRNAi; 55080; -.
DR Pharos; Q9BX59; Tbio.
DR PRO; PR:Q9BX59; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BX59; protein.
DR Bgee; ENSG00000139192; Expressed in granulocyte and 171 other tissues.
DR ExpressionAtlas; Q9BX59; baseline and differential.
DR Genevisible; Q9BX59; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0023024; F:MHC class I protein complex binding; IDA:UniProtKB.
DR GO; GO:0002590; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class I; IDA:UniProtKB.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IDA:UniProtKB.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Golgi apparatus; Immunity; Immunoglobulin domain; Membrane; Microsome;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 19..468
FT /note="Tapasin-related protein"
FT /id="PRO_0000014993"
FT TOPO_DOM 19..405
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 181..297
FT /note="Ig-like V-type"
FT DOMAIN 304..394
FT /note="Ig-like C1-type"
FT REGION 449..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 212..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 321..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 189..402
FT /note="Missing (in isoform epsilon)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057089"
FT VAR_SEQ 236..298
FT /note="QLVYSWTAGQGQAVRKGATLEPAQLGMARDASLTLPGLTIQDEGTYICQITT
FT SLYRAQQIIQL -> RGDLHLPDHHLSVPSSADHPAQHPRAENSLGSHLCQQSLPSCTD
FT VPGASETASTYRTWAASG (in isoform eta)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057090"
FT VAR_SEQ 236..262
FT /note="QLVYSWTAGQGQAVRKGATLEPAQLGM -> RGDLHLPDHHLSVPSSADHPA
FT QHPSFP (in isoform delta)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057091"
FT VAR_SEQ 263..468
FT /note="Missing (in isoform delta)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057092"
FT VAR_SEQ 299..468
FT /note="Missing (in isoform eta)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057093"
FT VAR_SEQ 302..402
FT /note="Missing (in isoform gamma)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057094"
FT VAR_SEQ 430..468
FT /note="QAPTGLGLLQAERWETTSCADTQSSHLHEDRTARVSQPS -> QEASAFLHC
FT APWAHAPRQRTGRSEGTRRRQNVQMEDKTKEPGWWCDGRKTKLEEMEKEQVRDNEAWVG
FT AGLPLPNSALSK (in isoform zeta)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057095"
FT VAR_SEQ 430
FT /note="Q -> QEASAFLHCAPWAHAPRQRTGRSEGTRRRQNVQMEDKTKEP (in
FT isoform beta)"
FT /evidence="ECO:0000303|PubMed:24444341"
FT /id="VSP_057096"
FT VARIANT 42
FT /note="A -> V (in dbSNP:rs2041385)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_071757"
FT VARIANT 146
FT /note="M -> V (in dbSNP:rs2532501)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_071758"
FT VARIANT 151
FT /note="G -> R (in dbSNP:rs7295376)"
FT /evidence="ECO:0000269|PubMed:11920573,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_033627"
FT VARIANT 165
FT /note="T -> A (in dbSNP:rs2532500)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_071759"
FT VARIANT 169
FT /note="A -> V (in dbSNP:rs2041387)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_071760"
FT VARIANT 334
FT /note="T -> M (in dbSNP:rs1045546)"
FT /evidence="ECO:0000269|PubMed:11920573"
FT /id="VAR_056090"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:5WER"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:5WER"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 318..329
FT /evidence="ECO:0007829|PDB:5WER"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:5WER"
SQ SEQUENCE 468 AA; 50183 MW; FA39C335FC22960E CRC64;
MGTQEGWCLL LCLALSGAAE TKPHPAEGQW RAVDVVLDCF LAKDGAHRGA LASSEDRARA
SLVLKQVPVL DDGSLEDFTD FQGGTLAQDD PPIIFEASVD LVQIPQAEAL LHADCSGKEV
TCEISRYFLQ MTETTVKTAA WFMANMQVSG GGPSISLVMK TPRVTKNEAL WHPTLNLPLS
PQGTVRTAVE FQVMTQTQSL SFLLGSSASL DCGFSMAPGL DLISVEWRLQ HKGRGQLVYS
WTAGQGQAVR KGATLEPAQL GMARDASLTL PGLTIQDEGT YICQITTSLY RAQQIIQLNI
QASPKVRLSL ANEALLPTLI CDIAGYYPLD VVVTWTREEL GGSPAQVSGA SFSSLRQSVA
GTYSISSSLT AEPGSAGATY TCQVTHISLE EPLGASTQVV PPERRTALGV IFASSLFLLA
LMFLGLQRRQ APTGLGLLQA ERWETTSCAD TQSSHLHEDR TARVSQPS
