TAPT1_HUMAN
ID TAPT1_HUMAN Reviewed; 567 AA.
AC Q6NXT6; Q8N2S3; Q9NZK9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transmembrane anterior posterior transformation protein 1 homolog;
DE AltName: Full=Cytomegalovirus partial fusion receptor;
GN Name=TAPT1; Synonyms=CMVFR;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-205, AND POSSIBLE FUNCTION FOR FUSION WITH
RP HCMV (MICROBIAL INFECTION).
RC TISSUE=Lung;
RX PubMed=10640539; DOI=10.1099/0022-1317-81-1-27;
RA Baldwin B.R., Zhang C.-O., Keay S.;
RT "Cloning and epitope mapping of a functional partial fusion receptor for
RT human cytomegalovirus gH.";
RL J. Gen. Virol. 81:27-35(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP VARIANT OCLSBG VAL-353, CHARACTERIZATION OF VARIANT OCLSBG VAL-353,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26365339; DOI=10.1016/j.ajhg.2015.08.009;
RA Symoens S., Barnes A.M., Gistelinck C., Malfait F., Guillemyn B.,
RA Steyaert W., Syx D., D'hondt S., Biervliet M., De Backer J., Witten E.P.,
RA Leikin S., Makareeva E., Gillessen-Kaesbach G., Huysseune A., Vleminckx K.,
RA Willaert A., De Paepe A., Marini J.C., Coucke P.J.;
RT "Genetic Defects in TAPT1 Disrupt Ciliogenesis and Cause a Complex Lethal
RT Osteochondrodysplasia.";
RL Am. J. Hum. Genet. 97:521-534(2015).
CC -!- FUNCTION: Plays a role in primary cilia formation (PubMed:26365339).
CC May act as a downstream effector of HOXC8 possibly by transducing or
CC transmitting extracellular information required for axial skeletal
CC patterning during development (By similarity). May be involved in
CC cartilage and bone development (By similarity). May play a role in the
CC differentiation of cranial neural crest cells (By similarity).
CC {ECO:0000250|UniProtKB:A2BIE7, ECO:0000250|UniProtKB:Q4VBD2,
CC ECO:0000269|PubMed:26365339}.
CC -!- FUNCTION: (Microbial infection) In case of infection, may act as a
CC fusion receptor for cytomegalovirus (HCMV) strain AD169.
CC {ECO:0000269|PubMed:10640539}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:26365339}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:26365339}. Membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NXT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NXT6-2; Sequence=VSP_032842;
CC -!- DISEASE: Osteochondrodysplasia, complex lethal, Symoens-Barnes-
CC Gistelinck type (OCLSBG) [MIM:616897]: An autosomal recessive, lethal
CC syndrome characterized by severe hypomineralization of the entire
CC skeleton, severe osteopenia, microcephaly, multiple intra-uterine
CC fractures, and multiple congenital developmental anomalies affecting
CC the brain, lungs, and kidneys. {ECO:0000269|PubMed:26365339}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TAPT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28308.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK074494; BAC11022.1; -; mRNA.
DR EMBL; CH471069; EAW92754.1; -; Genomic_DNA.
DR EMBL; BC066899; AAH66899.1; -; mRNA.
DR EMBL; AF189251; AAF28308.1; ALT_FRAME; mRNA.
DR CCDS; CCDS47030.1; -. [Q6NXT6-1]
DR RefSeq; NP_699196.2; NM_153365.2. [Q6NXT6-1]
DR AlphaFoldDB; Q6NXT6; -.
DR BioGRID; 128412; 48.
DR IntAct; Q6NXT6; 9.
DR STRING; 9606.ENSP00000385347; -.
DR iPTMnet; Q6NXT6; -.
DR PhosphoSitePlus; Q6NXT6; -.
DR SwissPalm; Q6NXT6; -.
DR BioMuta; TAPT1; -.
DR DMDM; 74737002; -.
DR EPD; Q6NXT6; -.
DR jPOST; Q6NXT6; -.
DR MassIVE; Q6NXT6; -.
DR MaxQB; Q6NXT6; -.
DR PaxDb; Q6NXT6; -.
DR PeptideAtlas; Q6NXT6; -.
DR PRIDE; Q6NXT6; -.
DR ProteomicsDB; 66775; -. [Q6NXT6-1]
DR ProteomicsDB; 66776; -. [Q6NXT6-2]
DR Antibodypedia; 54863; 84 antibodies from 19 providers.
DR DNASU; 202018; -.
DR Ensembl; ENST00000405303.7; ENSP00000385347.2; ENSG00000169762.17. [Q6NXT6-1]
DR GeneID; 202018; -.
DR KEGG; hsa:202018; -.
DR MANE-Select; ENST00000405303.7; ENSP00000385347.2; NM_153365.3; NP_699196.2.
DR UCSC; uc010ied.2; human. [Q6NXT6-1]
DR CTD; 202018; -.
DR DisGeNET; 202018; -.
DR GeneCards; TAPT1; -.
DR HGNC; HGNC:26887; TAPT1.
DR HPA; ENSG00000169762; Low tissue specificity.
DR MalaCards; TAPT1; -.
DR MIM; 612758; gene.
DR MIM; 616897; phenotype.
DR neXtProt; NX_Q6NXT6; -.
DR OpenTargets; ENSG00000169762; -.
DR Orphanet; 457378; Complex lethal osteochondrodysplasia.
DR PharmGKB; PA162405167; -.
DR VEuPathDB; HostDB:ENSG00000169762; -.
DR eggNOG; KOG2490; Eukaryota.
DR GeneTree; ENSGT00390000010628; -.
DR HOGENOM; CLU_003655_3_0_1; -.
DR InParanoid; Q6NXT6; -.
DR OMA; SYFMMHY; -.
DR OrthoDB; 572763at2759; -.
DR PhylomeDB; Q6NXT6; -.
DR TreeFam; TF105962; -.
DR PathwayCommons; Q6NXT6; -.
DR SignaLink; Q6NXT6; -.
DR BioGRID-ORCS; 202018; 85 hits in 1096 CRISPR screens.
DR ChiTaRS; TAPT1; human.
DR GenomeRNAi; 202018; -.
DR Pharos; Q6NXT6; Tbio.
DR PRO; PR:Q6NXT6; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6NXT6; protein.
DR Bgee; ENSG00000169762; Expressed in secondary oocyte and 185 other tissues.
DR ExpressionAtlas; Q6NXT6; baseline and differential.
DR Genevisible; Q6NXT6; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; TAS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:1903012; P:positive regulation of bone development; ISS:UniProtKB.
DR GO; GO:0061036; P:positive regulation of cartilage development; ISS:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IDA:UniProtKB.
DR InterPro; IPR008010; Tatp1.
DR PANTHER; PTHR13317; PTHR13317; 1.
DR Pfam; PF05346; DUF747; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Chondrogenesis;
KW Ciliopathy; Cilium; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Disease variant;
KW Host-virus interaction; Membrane; Osteogenesis; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..567
FT /note="Transmembrane anterior posterior transformation
FT protein 1 homolog"
FT /id="PRO_0000328872"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4VBD2"
FT VAR_SEQ 551..567
FT /note="KDLLEIDRFTICGNRID -> SVLLCQSGLPEC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_032842"
FT VARIANT 353
FT /note="D -> V (in OCLSBG; causes mislocalization of the
FT protein in the cytoplasm; impairs cilium formation;
FT dbSNP:rs869312980)"
FT /evidence="ECO:0000269|PubMed:26365339"
FT /id="VAR_076497"
FT VARIANT 465
FT /note="E -> K (in dbSNP:rs35606284)"
FT /id="VAR_042568"
FT VARIANT 522
FT /note="N -> S (in dbSNP:rs16893137)"
FT /id="VAR_042569"
FT CONFLICT 30
FT /note="E -> D (in Ref. 1; BAC11022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 64260 MW; 2EAB6EF6A7A40E71 CRC64;
MAGVGDAAAP GEGGGGGVDG PQRDGRGEAE QPGGSGGQGP PPAPQLTETL GFYESDRRRE
RRRGRTELSL LRFLSAELTR GYFLEHNEAK YTERRERVYT CLRIPRELEK LMVFGIFLCL
DAFLYVFTLL PLRVFLALFR LLTLPCYGLR DRRLLQPAQV CDILKGVILV ICYFMMHYVD
YSMMYHLIRG QSVIKLYIIY NMLEVADRLF SSFGQDILDA LYWTATEPKE RKRAHIGVIP
HFFMAVLYVF LHAILIMVQA TTLNVAFNSH NKSLLTIMMS NNFVEIKGSV FKKFEKNNLF
QMSNSDIKER FTNYVLLLIV CLRNMEQFSW NPDHLWVLFP DVCMVIASEI AVDIVKHAFI
TKFNDITADV YSEYRASLAF DLVSSRQKNA YTDYSDSVAR RMGFIPLPLA VLLIRVVTSS
IKVQGILSYA CVILFYFGLI SLKVLNSIVL LGKSCQYVKE AKMEEKLSNP PATCTPGKPS
SKSQNKCKPS QGLSTEENLS ASITKQPIHQ KENIIPLLVT SNSDQFLTTP DGDEKDITQD
NSELKHRSSK KDLLEIDRFT ICGNRID
