ID   TEKT4_BOVIN             Reviewed;         447 AA.
AC   Q2TA38;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tektin-4;
GN   Name=TEKT4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007744|PDB:7RRO}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=34715025; DOI=10.1016/j.cell.2021.10.007;
RA   Gui M., Farley H., Anujan P., Anderson J.R., Maxwell D.W., Whitchurch J.B.,
RA   Botsch J.J., Qiu T., Meleppattu S., Singh S.K., Zhang Q., Thompson J.,
RA   Lucas J.S., Bingle C.D., Norris D.P., Roy S., Brown A.;
RT   "De novo identification of mammalian ciliary motility proteins using cryo-
RT   EM.";
RL   Cell 184:5791-5806.e19(2021).
CC   -!- FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated
CC       doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms
CC       filamentous polymers in the walls of ciliary and flagellar microtubules
CC       (PubMed:34715025). Contributes to normal sperm motility (By
CC       similarity). {ECO:0000250|UniProtKB:Q6X6Z7,
CC       ECO:0000269|PubMed:34715025}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:34715025}. Cell projection, cilium, flagellum
CC       {ECO:0000250|UniProtKB:Q149S1}. Note=Found in the abaxial (convex)
CC       surface of outer dense fibers in sperm flagella.
CC       {ECO:0000250|UniProtKB:Q149S1}.
CC   -!- TISSUE SPECIFICITY: Expressed in trachea multiciliated cells.
CC       {ECO:0000269|PubMed:34715025}.
CC   -!- SIMILARITY: Belongs to the tektin family. {ECO:0000305}.
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DR   EMBL; BC111132; AAI11133.1; -; mRNA.
DR   RefSeq; NP_001033158.1; NM_001038069.2.
DR   PDB; 7RRO; EM; 3.40 A; D0/D1/D2/D3/D5/D6/D7/D8/D9=1-447.
DR   PDBsum; 7RRO; -.
DR   AlphaFoldDB; Q2TA38; -.
DR   SMR; Q2TA38; -.
DR   STRING; 9913.ENSBTAP00000016726; -.
DR   PaxDb; Q2TA38; -.
DR   Ensembl; ENSBTAT00000016726; ENSBTAP00000016726; ENSBTAG00000012601.
DR   GeneID; 510343; -.
DR   KEGG; bta:510343; -.
DR   CTD; 150483; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012601; -.
DR   VGNC; VGNC:99678; TEKT4.
DR   eggNOG; KOG2685; Eukaryota.
DR   GeneTree; ENSGT00950000182894; -.
DR   HOGENOM; CLU_033588_2_1_1; -.
DR   InParanoid; Q2TA38; -.
DR   OMA; RNLEDTH; -.
DR   OrthoDB; 581072at2759; -.
DR   TreeFam; TF320754; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000012601; Expressed in spermatid and 23 other tissues.
DR   ExpressionAtlas; Q2TA38; baseline.
DR   GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0036126; C:sperm flagellum; IBA:GO_Central.
DR   GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR   GO; GO:0097228; C:sperm principal piece; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR   GO; GO:0060378; P:regulation of brood size; IEA:Ensembl.
DR   InterPro; IPR000435; Tektin.
DR   PANTHER; PTHR19960; PTHR19960; 1.
DR   PRINTS; PR00511; TEKTIN.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Flagellum; Reference proteome.
FT   CHAIN           1..447
FT                   /note="Tektin-4"
FT                   /id="PRO_0000261174"
FT   REGION          72..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          69..144
FT                   /evidence="ECO:0000255"
FT   COILED          304..423
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        84..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  51945 MW;  BC240F29C946EB38 CRC64;
     MAQTDILLTK EPAPQTVPAC QLPRKLYDVA RNTGAHTSSG LATSGFRTAK YLLDEWFQNC
     YARYHQAFAD RDQSERQRHE SQQLAAETEA LAQRTQQDST RKVGERLQDM HGWKSELQRQ
     VEELVSETEL LLAQKQRLER ALDATAGPFS IVTDNLQCRE RRQHPDLVRD CVEIELLKEA
     ELIRNIQELL KRTIKQAVSQ IRLNWEHKET CEMDWSDKVE AYNIDEACCR YNNQSTDVQF
     YPHSAKFEES ASTPETWAKF TQEHLYRAER ERLASVNLRN LIDCILQDTS EDLRLQCDAV
     NLAFGRRCEE LEDARHKLEH HLRKTLREIS DQEHNIAALK QAIKDKEAPL KVAQTRLYQR
     SHRPNVELCR DAAQFRLASE VEELNLSLAA LKEKLLEAEQ SLRNLEDTRM SLEKDIAIKT
     NSLFIDRHKC MAHRAHYPTV LQLAGYQ