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Transmembrane anterior posterior transformation protein 1 homolog (Cytomegalovirus partial fusion receptor)

 TAPT1_HUMAN             Reviewed;         567 AA.
Q6NXT6; Q8N2S3; Q9NZK9;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
20-JUN-2018, entry version 104.
RecName: Full=Transmembrane anterior posterior transformation protein 1 homolog;
AltName: Full=Cytomegalovirus partial fusion receptor;
Name=TAPT1; Synonyms=CMVFR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Embryo;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-205, AND POSSIBLE FUNCTION FOR FUSION
WITH HCMV (MICROBIAL INFECTION).
TISSUE=Lung;
PubMed=10640539;
Baldwin B.R., Zhang C.-O., Keay S.;
"Cloning and epitope mapping of a functional partial fusion receptor
for human cytomegalovirus gH.";
J. Gen. Virol. 81:27-35(2000).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
VARIANT OCLSBG VAL-353, CHARACTERIZATION OF VARIANT OCLSBG VAL-353,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26365339; DOI=10.1016/j.ajhg.2015.08.009;
Symoens S., Barnes A.M., Gistelinck C., Malfait F., Guillemyn B.,
Steyaert W., Syx D., D'hondt S., Biervliet M., De Backer J.,
Witten E.P., Leikin S., Makareeva E., Gillessen-Kaesbach G.,
Huysseune A., Vleminckx K., Willaert A., De Paepe A., Marini J.C.,
Coucke P.J.;
"Genetic Defects in TAPT1 Disrupt Ciliogenesis and Cause a Complex
Lethal Osteochondrodysplasia.";
Am. J. Hum. Genet. 97:521-534(2015).
-!- FUNCTION: Plays a role in primary cilia formation
(PubMed:26365339). May act as a downstream effector of HOXC8
possibly by transducing or transmitting extracellular information
required for axial skeletal patterning during development (By
similarity). May be involved in cartilage and bone development (By
similarity). May play a role in the differentiation of cranial
neural crest cells (By similarity). {ECO:0000250|UniProtKB:A2BIE7,
ECO:0000250|UniProtKB:Q4VBD2, ECO:0000269|PubMed:26365339}.
-!- FUNCTION: (Microbial infection) In case of infection, may act as a
fusion receptor for cytomegalovirus (HCMV) strain AD169.
{ECO:0000269|PubMed:10640539}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:26365339}.
Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000269|PubMed:26365339}. Membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6NXT6-1; Sequence=Displayed;
Name=2;
IsoId=Q6NXT6-2; Sequence=VSP_032842;
Note=No experimental confirmation available.;
-!- DISEASE: Osteochondrodysplasia, complex lethal, Symoens-Barnes-
Gistelinck type (OCLSBG) [MIM:616897]: An autosomal recessive,
lethal syndrome characterized by severe hypomineralization of the
entire skeleton, severe osteopenia, microcephaly, multiple intra-
uterine fractures, and multiple congenital developmental anomalies
affecting the brain, lungs, and kidneys.
{ECO:0000269|PubMed:26365339}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TAPT1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF28308.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK074494; BAC11022.1; -; mRNA.
EMBL; CH471069; EAW92754.1; -; Genomic_DNA.
EMBL; BC066899; AAH66899.1; -; mRNA.
EMBL; AF189251; AAF28308.1; ALT_FRAME; mRNA.
CCDS; CCDS47030.1; -. [Q6NXT6-1]
RefSeq; NP_699196.2; NM_153365.2. [Q6NXT6-1]
UniGene; Hs.479223; -.
ProteinModelPortal; Q6NXT6; -.
SMR; Q6NXT6; -.
BioGrid; 128412; 8.
IntAct; Q6NXT6; 3.
STRING; 9606.ENSP00000385347; -.
iPTMnet; Q6NXT6; -.
PhosphoSitePlus; Q6NXT6; -.
SwissPalm; Q6NXT6; -.
BioMuta; TAPT1; -.
DMDM; 74737002; -.
EPD; Q6NXT6; -.
MaxQB; Q6NXT6; -.
PaxDb; Q6NXT6; -.
PeptideAtlas; Q6NXT6; -.
PRIDE; Q6NXT6; -.
ProteomicsDB; 66775; -.
ProteomicsDB; 66776; -. [Q6NXT6-2]
Ensembl; ENST00000405303; ENSP00000385347; ENSG00000169762. [Q6NXT6-1]
GeneID; 202018; -.
KEGG; hsa:202018; -.
UCSC; uc010ied.2; human. [Q6NXT6-1]
CTD; 202018; -.
DisGeNET; 202018; -.
EuPathDB; HostDB:ENSG00000169762.16; -.
GeneCards; TAPT1; -.
HGNC; HGNC:26887; TAPT1.
HPA; HPA042567; -.
HPA; HPA048658; -.
MalaCards; TAPT1; -.
MIM; 612758; gene.
MIM; 616897; phenotype.
neXtProt; NX_Q6NXT6; -.
OpenTargets; ENSG00000169762; -.
PharmGKB; PA162405167; -.
eggNOG; KOG2490; Eukaryota.
eggNOG; ENOG410XT6F; LUCA.
GeneTree; ENSGT00390000010628; -.
HOGENOM; HOG000154508; -.
HOVERGEN; HBG108546; -.
InParanoid; Q6NXT6; -.
OMA; EKLFDPP; -.
OrthoDB; EOG091G07IY; -.
PhylomeDB; Q6NXT6; -.
TreeFam; TF105962; -.
ChiTaRS; TAPT1; human.
GenomeRNAi; 202018; -.
PRO; PR:Q6NXT6; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000169762; -.
CleanEx; HS_TAPT1; -.
ExpressionAtlas; Q6NXT6; baseline and differential.
Genevisible; Q6NXT6; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; TAS:UniProtKB.
GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:1903012; P:positive regulation of bone development; ISS:UniProtKB.
GO; GO:0061036; P:positive regulation of cartilage development; ISS:UniProtKB.
GO; GO:0045724; P:positive regulation of cilium assembly; IDA:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
InterPro; IPR008010; Tatp1.
PANTHER; PTHR13317; PTHR13317; 1.
Pfam; PF05346; DUF747; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell projection; Chondrogenesis;
Ciliopathy; Cilium; Cilium biogenesis/degradation; Complete proteome;
Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
Disease mutation; Membrane; Osteogenesis; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 567 Transmembrane anterior posterior
transformation protein 1 homolog.
/FTId=PRO_0000328872.
TRANSMEM 111 131 Helical. {ECO:0000255}.
TRANSMEM 157 179 Helical. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TRANSMEM 403 423 Helical. {ECO:0000255}.
TRANSMEM 432 452 Helical. {ECO:0000255}.
COMPBIAS 3 39 Gly-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 529 529 Phosphothreonine.
{ECO:0000250|UniProtKB:Q4VBD2}.
VAR_SEQ 551 567 KDLLEIDRFTICGNRID -> SVLLCQSGLPEC (in
isoform 2).
{ECO:0000303|PubMed:16303743}.
/FTId=VSP_032842.
VARIANT 353 353 D -> V (in OCLSBG; causes mislocalization
of the protein in the cytoplasm; impairs
cilium formation; dbSNP:rs869312980).
{ECO:0000269|PubMed:26365339}.
/FTId=VAR_076497.
VARIANT 465 465 E -> K (in dbSNP:rs35606284).
/FTId=VAR_042568.
VARIANT 522 522 N -> S (in dbSNP:rs16893137).
/FTId=VAR_042569.
CONFLICT 30 30 E -> D (in Ref. 1; BAC11022).
{ECO:0000305}.
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


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