TAPT1_MOUSE
ID TAPT1_MOUSE Reviewed; 564 AA.
AC Q4VBD2; Q8CDI4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Transmembrane anterior posterior transformation protein 1;
GN Name=Tapt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-564.
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-564.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17151244; DOI=10.1534/genetics.106.065177;
RA Howell G.R., Shindo M., Murray S., Gridley T., Wilson L.A., Schimenti J.C.;
RT "Mutation of a ubiquitously expressed mouse transmembrane protein (Tapt1)
RT causes specific skeletal homeotic transformations.";
RL Genetics 175:699-707(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND THR-526, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in primary cilia formation (By similarity). May
CC 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:Q6NXT6,
CC ECO:0000269|PubMed:17151244}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q6NXT6}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6NXT6}.
CC Membrane {ECO:0000250|UniProtKB:Q6NXT6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6NXT6}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed throughout embryo.
CC {ECO:0000269|PubMed:17151244}.
CC -!- DISRUPTION PHENOTYPE: Mice die during perinatal development and are the
CC cause of the L5Jcs1 phenotype. They exhibit posterior-to-anterior
CC transformations of the vertebral column midsection, similar to mice
CC deficient for Hoxc8 and Hoxc9. {ECO:0000269|PubMed:17151244}.
CC -!- SIMILARITY: Belongs to the TAPT1 family. {ECO:0000305}.
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DR EMBL; AC103621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096038; AAH96038.1; -; mRNA.
DR EMBL; AK030002; BAC26728.1; -; mRNA.
DR CCDS; CCDS19270.1; -.
DR RefSeq; NP_776125.2; NM_173764.3.
DR AlphaFoldDB; Q4VBD2; -.
DR BioGRID; 231097; 12.
DR IntAct; Q4VBD2; 9.
DR STRING; 10090.ENSMUSP00000062110; -.
DR iPTMnet; Q4VBD2; -.
DR PhosphoSitePlus; Q4VBD2; -.
DR SwissPalm; Q4VBD2; -.
DR EPD; Q4VBD2; -.
DR jPOST; Q4VBD2; -.
DR MaxQB; Q4VBD2; -.
DR PaxDb; Q4VBD2; -.
DR PeptideAtlas; Q4VBD2; -.
DR PRIDE; Q4VBD2; -.
DR ProteomicsDB; 254816; -.
DR Antibodypedia; 54863; 84 antibodies from 19 providers.
DR DNASU; 231225; -.
DR Ensembl; ENSMUST00000055128; ENSMUSP00000062110; ENSMUSG00000046985.
DR GeneID; 231225; -.
DR KEGG; mmu:231225; -.
DR UCSC; uc008xin.1; mouse.
DR CTD; 202018; -.
DR MGI; MGI:2683537; Tapt1.
DR VEuPathDB; HostDB:ENSMUSG00000046985; -.
DR eggNOG; KOG2490; Eukaryota.
DR GeneTree; ENSGT00390000010628; -.
DR HOGENOM; CLU_003655_3_0_1; -.
DR InParanoid; Q4VBD2; -.
DR OMA; SYFMMHY; -.
DR OrthoDB; 572763at2759; -.
DR PhylomeDB; Q4VBD2; -.
DR TreeFam; TF105962; -.
DR BioGRID-ORCS; 231225; 10 hits in 73 CRISPR screens.
DR ChiTaRS; Tapt1; mouse.
DR PRO; PR:Q4VBD2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q4VBD2; protein.
DR Bgee; ENSMUSG00000046985; Expressed in facial nucleus and 224 other tissues.
DR ExpressionAtlas; Q4VBD2; baseline and differential.
DR Genevisible; Q4VBD2; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048856; P:anatomical structure development; IMP:MGI.
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; IMP:MGI.
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; ISS:UniProtKB.
DR InterPro; IPR008010; Tatp1.
DR PANTHER; PTHR13317; PTHR13317; 1.
DR Pfam; PF05346; DUF747; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Chondrogenesis; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Membrane; Osteogenesis;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6NXT6"
FT CHAIN 2..564
FT /note="Transmembrane anterior posterior transformation
FT protein 1"
FT /id="PRO_0000328873"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXT6"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 564 AA; 63894 MW; 97D28BC7970C61C2 CRC64;
MAGVCDAAAP GEGGGGGADG PERTGRGEAE QPGGGGHGPA PQHTETLGFY ESDRRREKRR
GRAELSLLRF LSAELTRGYF LEHNEAKYTE RRERVYTCMR IPRELEKLMF FGIFLCLDAF
LYVFTLLPLR VFLALFRLLT LPCYGLRDRR LLQPAQVCDI LKGVILVICY FMMHYVDYSM
MYHLIRGQSV IKLYIIYNML EVADRLFSSF GQDILDALYW TATEPKERKR AHIGVIPHFF
MAVLYVFLHA ILIMVQATTL NVAFNSHNKS LLTIMMSNNF VEIKGSVFKK FEKNNLFQMS
NSDIKERFTN YVLLLIVCLR NMEQFSWNPD HLWVLFPDVC MVIASEIAVD IVKHAFITKF
NDITADVYSE YRASLAFDLV SSRQKNAYTD YSDSVARRMG FIPLPLAVLL IRVVTSSIKV
QGILSYACVI LFYFGLISLK ILNSIVLLGK SCQYVKEAKM EEKLFNPPPA STPGKPSSKS
QSKGKPSQGL STEENLSASV TSQPGHQKEN VIPLLVTSNS DQFLTTPDGD EKDITQENSE
LKHRSSKKDL LEIDRFTICG NRID
