TEKT3_MOUSE
ID TEKT3_MOUSE Reviewed; 490 AA.
AC Q6X6Z7;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Tektin-3;
GN Name=Tekt3;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X 129; TISSUE=Testis;
RX PubMed=14735490; DOI=10.1002/mrd.20025;
RA Roy A., Yan W., Burns K.H., Matzuk M.M.;
RT "Tektin3 encodes an evolutionarily conserved putative testicular
RT microtubules-related protein expressed preferentially in male germ cells.";
RL Mol. Reprod. Dev. 67:295-302(2004).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18951373; DOI=10.1002/mrd.20957;
RA Roy A., Lin Y.-N., Agno J.E., DeMayo F.J., Matzuk M.M.;
RT "Tektin 3 is required for progressive sperm motility in mice.";
RL Mol. Reprod. Dev. 76:453-459(2009).
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 (By similarity). Required for normal sperm mobility (PubMed:18951373).
CC {ECO:0000250|UniProtKB:A6H782, ECO:0000269|PubMed:18951373}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:A6H782}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q4V8G8}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane
CC {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q4V8G8};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q4V8G8}. Note=In the
CC sperm flagellum, localizes to the periaxonemal region where it
CC associates with the mitochondrial sheath and outer dense fibers (By
CC similarity). Not detected in the central axonemal region of the
CC flagellum (By similarity). Associates with the acrosome membrane in the
CC equatorial segment of the sperm head (By similarity). Also detected
CC just below the plasma membrane in the post-acrosomal region where it
CC might localize to the postacrosomal dense lamina (By similarity).
CC However, other studies report little or no expression in the
CC postacrosomal region (By similarity). Translocates from the
CC postacrosomal region to the equatorial segment after sperm activation
CC (By similarity). Retained in the postacromal region, but not the
CC equatorial segment, following the acrosome reaction (By similarity).
CC Some studies report strong expression in the anterior cap region (By
CC similarity). However, other studies report little or no expression in
CC the acrosomal cap (By similarity). {ECO:0000250|UniProtKB:A6H782,
CC ECO:0000250|UniProtKB:Q4V8G8}.
CC -!- TISSUE SPECIFICITY: Expressed preferentially in testis. Expressed
CC predominantly in late pachytene spermatocytes and early round
CC spermatids. {ECO:0000269|PubMed:14735490}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:A6H782}.
CC -!- PTM: May be proteolytically processed during the epididymal transit of
CC spermatozoa. {ECO:0000250|UniProtKB:A6H782}.
CC -!- DISRUPTION PHENOTYPE: Sperm with reduced motility (47%) and forward
CC progression and increased flagellar structural bending defects.
CC However, normal fertility is maintained. {ECO:0000269|PubMed:18951373}.
CC -!- SIMILARITY: Belongs to the tektin family. {ECO:0000305}.
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DR EMBL; AY252101; AAP86970.1; -; mRNA.
DR CCDS; CCDS24836.1; -.
DR RefSeq; NP_081936.1; NM_027660.1.
DR AlphaFoldDB; Q6X6Z7; -.
DR SMR; Q6X6Z7; -.
DR BioGRID; 214445; 1.
DR STRING; 10090.ENSMUSP00000042063; -.
DR GlyGen; Q6X6Z7; 7 sites.
DR iPTMnet; Q6X6Z7; -.
DR PhosphoSitePlus; Q6X6Z7; -.
DR MaxQB; Q6X6Z7; -.
DR PaxDb; Q6X6Z7; -.
DR PRIDE; Q6X6Z7; -.
DR ProteomicsDB; 262974; -.
DR Antibodypedia; 25125; 144 antibodies from 21 providers.
DR DNASU; 71062; -.
DR Ensembl; ENSMUST00000035732; ENSMUSP00000042063; ENSMUSG00000042189.
DR GeneID; 71062; -.
DR KEGG; mmu:71062; -.
DR UCSC; uc007jkl.1; mouse.
DR CTD; 64518; -.
DR MGI; MGI:1918312; Tekt3.
DR VEuPathDB; HostDB:ENSMUSG00000042189; -.
DR eggNOG; KOG2685; Eukaryota.
DR GeneTree; ENSGT00950000182894; -.
DR HOGENOM; CLU_033588_2_1_1; -.
DR InParanoid; Q6X6Z7; -.
DR OMA; QRIDDRC; -.
DR OrthoDB; 581072at2759; -.
DR PhylomeDB; Q6X6Z7; -.
DR TreeFam; TF320754; -.
DR BioGRID-ORCS; 71062; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Tekt3; mouse.
DR PRO; PR:Q6X6Z7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6X6Z7; protein.
DR Bgee; ENSMUSG00000042189; Expressed in seminiferous tubule of testis and 10 other tissues.
DR ExpressionAtlas; Q6X6Z7; baseline and differential.
DR Genevisible; Q6X6Z7; MM.
DR GO; GO:0002080; C:acrosomal membrane; ISS:CAFA.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; IMP:UniProtKB.
DR GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; IGI:UniProtKB.
DR InterPro; IPR000435; Tektin.
DR PANTHER; PTHR19960; PTHR19960; 1.
DR PRINTS; PR00511; TEKTIN.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Flagellum; Glycoprotein; Membrane; Reference proteome.
FT CHAIN 1..490
FT /note="Tektin-3"
FT /id="PRO_0000184569"
FT COILED 415..461
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 11
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 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; 56673 MW; C09CA9491D501C15 CRC64;
MELLGSTLTA TYAHPPPASA SFLPAIGTIT SSYKDRFPHR NLTHSLSLPW RPNTYYKTAY
NYPTLAPYSS RSQRVCESTM LPFVSNRTTF FTRYTPDDWY RSNLVSFQES NSSRHNSERL
RVDTSRLIQD KYQQIRKTQA HSTQNLGERV NDLAFWKSEI THELDEMIGE TNALTDIKRR
LERGLIETEG PLQVSRECLF HREKRMGIDL VHDEAEKELL AEVDTILCCQ ERMRQHLDKA
NAQLASDRSA QHELEKDLSD KQAALRIDDK CQHLRNTSEG VSYFRGVERV DATVSVPETW
AKFTDDNVLR SQSERAASAK LREETENLLI VTANEMWNQF NKVNLAFTNR IAETVDAKNK
IHTHLTKTLQ EIFQIEMTIE SIKKAIKEKS AFLKVAQTRL DERTRRPNVE LCRDMAQLRL
VNEVYEVDET IQTLQQRLRD SEDTLQSLAH TKATLEHDLA VKANTLYIDQ EKCMSMRNSY
PSTLRLVGYC
