ID   TAPT1_XENLA             Reviewed;         546 AA.
AC   Q5EAY8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Transmembrane anterior posterior transformation protein 1 homolog;
GN   Name=tapt1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in primary cilia formation. Involved in
CC       cartilage and bone development. May play a role in the differentiation
CC       of cranial neural crest cells. May act as a downstream effector of
CC       hoxc8 during development. {ECO:0000250|UniProtKB:A2BIE7,
CC       ECO:0000250|UniProtKB:Q4VBD2}.
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   -!- SIMILARITY: Belongs to the TAPT1 family. {ECO:0000305}.
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DR   EMBL; BC090195; AAH90195.1; -; mRNA.
DR   RefSeq; NP_001089274.1; NM_001095805.1.
DR   AlphaFoldDB; Q5EAY8; -.
DR   DNASU; 734322; -.
DR   GeneID; 734322; -.
DR   KEGG; xla:734322; -.
DR   CTD; 734322; -.
DR   OrthoDB; 572763at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 734322; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell projection; Chondrogenesis; Cilium; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Membrane;
KW   Osteogenesis; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..546
FT                   /note="Transmembrane anterior posterior transformation
FT                   protein 1 homolog"
FT                   /id="PRO_0000328876"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  61795 MW;  657779F334A601DF CRC64;
     MADAAMSGEE KEEDGGKRTT AATPAETLGF YEPSDGSRVE TKKRSLSDLS LLRFISAELT
     RGYFLENNEA KYKERREKVY TCLRIPRELE KLMVFGFFLC LDAFLYVFTL LPLRVLLALI
     RFLTLPCCGL SDGRVLQPAQ VCDVLKGVIL VICYFIMHYV DYSMMYHLIR GQSVIKLYII
     YNMLEVADRL FSSFGQDILD ALYWTATEPK ERKRAHLGVI PHFFMAVLYV ILHAILILVQ
     ATTLNVAFNS HNKSLLTIMM SNNFVEIKGS VFKKFEKNNL FQMSNSDIKE RFTNYVLLLI
     VCLRNMEQFS WNPDHLWVLF PDVCMVIASE IAVDVVKHAF ITKFNDITAD VYSEYRASLA
     FELVSSRQKN ACTDYSDSVS RRMGFIPLPL AVLLIRVVTS SVKVQGILAY SCVVLFYFGL
     ITLKVLNSIV LLGKSCQYIK DANMEEKLFQ PPTCQPGKTP KKAQNKSKPN QGHPPDETAN
     TSVTSQPTKA ASTAQLLVES NSDKLLTTPD AEEKDISGDN SELKQKQADK DLLDIDRFTI
     CGNRID