TEKT3_BOVIN
ID TEKT3_BOVIN Reviewed; 490 AA.
AC A6H782;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Tektin-3 {ECO:0000303|PubMed:26268136};
GN Name=TEKT3 {ECO:0000303|PubMed:26268136};
GN Synonyms=OMC45 {ECO:0000303|PubMed:19478333};
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 (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19478333; DOI=10.2164/jandrol.108.007146;
RA Nagdas S.K., Hamilton S.L., Raychoudhury S.;
RT "Identification of acrosomal matrix-specific hydrolases binding proteins of
RT bovine cauda epididymal spermatozoa.";
RL J. Androl. 31:177-187(2010).
RN [3]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, POSSIBLE PROTEOLYTIC PROCESSING, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26268136; DOI=10.1007/s11010-015-2534-8;
RA Nagdas S.K., Smith L., Mcnamara A., Hernandez-Encarnacion L.,
RA Medina-Ortiz I.;
RT "Identification and characterization of a bovine sperm acrosomal matrix
RT protein and its mechanism of interaction with acrosomal hydrolases.";
RL Mol. Cell. Biochem. 410:11-23(2015).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27883267; DOI=10.1002/mrd.22763;
RA Tsukamoto M., Hiyama E., Hirotani K., Gotoh T., Inai T., Iida H.;
RT "Translocation of Tektin 3 to the equatorial segment of heads in bull
RT spermatozoa exposed to dibutyryl cAMP and calyculin A.";
RL Mol. Reprod. Dev. 84:30-43(2017).
RN [5] {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). Required for normal sperm mobility (By similarity).
CC {ECO:0000250|UniProtKB:Q6X6Z7, ECO:0000269|PubMed:34715025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:34715025}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:27883267}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome outer membrane {ECO:0000269|PubMed:19478333,
CC ECO:0000269|PubMed:26268136, ECO:0000269|PubMed:27883267}; Peripheral
CC membrane protein {ECO:0000305}. Note=In the sperm flagellum, localizes
CC to the periaxonemal region where it associates with the mitochondrial
CC sheath and outer dense fibers (By similarity). Not detected in the
CC central axonemal region of the flagellum (By similarity). Associates
CC with the acrosome membrane in the equatorial segment of the sperm head
CC (PubMed:27883267). Also detected just below the plasma membrane in the
CC post-acrosomal region where it might localize to the postacrosomal
CC dense lamina (PubMed:27883267). However, other studies report little or
CC no expression in the postacrosomal region (By similarity). Translocates
CC from the postacrosomal region to the equatorial segment after sperm
CC activation (PubMed:27883267). Retained in the postacromal region, but
CC not the equatorial segment, following the acrosome reaction
CC (PubMed:27883267). Some studies report strong expression in the
CC anterior acrosomal cap region (PubMed:19478333, PubMed:26268136).
CC However, other studies report little or no expression in the acrosomal
CC cap (PubMed:27883267). {ECO:0000250|UniProtKB:Q4V8G8,
CC ECO:0000269|PubMed:19478333, ECO:0000269|PubMed:26268136,
CC ECO:0000269|PubMed:27883267}.
CC -!- TISSUE SPECIFICITY: Expressed in spermatozoa where it localizes to the
CC sperm head (at protein level) (PubMed:19478333, PubMed:26268136).
CC Detected at lower levels in the sperm flagellum (at protein level)
CC (PubMed:27883267). Expressed in trachea multiciliated cells
CC (PubMed:34715025). {ECO:0000269|PubMed:19478333,
CC ECO:0000269|PubMed:26268136, ECO:0000269|PubMed:27883267,
CC ECO:0000269|PubMed:34715025}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:26268136}.
CC -!- PTM: May be proteolytically processed during the epididymal transit of
CC spermatozoa. {ECO:0000269|PubMed:26268136}.
CC -!- SIMILARITY: Belongs to the tektin family. {ECO:0000305}.
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DR EMBL; BC146148; AAI46149.1; -; mRNA.
DR RefSeq; NP_001092489.1; NM_001099019.2.
DR PDB; 7RRO; EM; 3.40 A; C0/C1/C2/C3/C4/C5/C6/C7/C8/C9/F0/F1/F2/F3/F4=1-490.
DR PDBsum; 7RRO; -.
DR AlphaFoldDB; A6H782; -.
DR SMR; A6H782; -.
DR STRING; 9913.ENSBTAP00000004942; -.
DR PaxDb; A6H782; -.
DR GeneID; 522915; -.
DR KEGG; bta:522915; -.
DR CTD; 64518; -.
DR eggNOG; KOG2685; Eukaryota.
DR InParanoid; A6H782; -.
DR OrthoDB; 581072at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0002080; C:acrosomal membrane; ISS:CAFA.
DR GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0002081; C:outer acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036126; C:sperm flagellum; ISS:CAFA.
DR GO; GO:0060271; P:cilium assembly; ISS:CAFA.
DR GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; ISS:UniProtKB.
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; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Flagellum; Glycoprotein; Membrane;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Tektin-3"
FT /id="PRO_0000380246"
FT COILED 424..458
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 9
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 56681 MW; 4039D7E393824477 CRC64;
MELLGSTLTA TYAHPRPTPT NFLPAISTMA STYRDRFPHY NLTHSLSLPW RPSTYYKAAS
NWPTLDPYCT RSQRVSESTM LPFVSNRTTL FTRYTPDDWY RSNLTNFQES NTSRHNSERL
RVDTSRLIQD KYQQTRKTQA DSTQNLGERV NDIGFWKSEI IHELDAMIGE TNELTDIKKR
LERALMETEA PLQVARECLF HREKRMGIDL VHDEVEKELL TEVDTILCCQ ERMKLYLDKA
IAQLAANRAA QHELEKDLSD KQSAYRIDDK CHHLRNTSDG VSYFHGVERV DATVSVPESW
AKFTDDNILR SQSERAASAK LRDDIQNVLV VTANEMWNQF NKVNLAFTNR IAETADAKNK
IQTHLAKTLQ EIFQTEMTIE SIKKAIVEKS AFLKVAQTRL DERTRRPNIE LCRDMAQLRL
VNEVYEVDDT IQTLQQRLRD AEDTLQSLAH TKATLEHDLA VKANSLYIDQ DKCMSMRRSF
PSTLRLVGFC
