TEKT3_RAT
ID TEKT3_RAT Reviewed; 490 AA.
AC Q4V8G8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Tektin-3;
GN Name=Tekt3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21744413; DOI=10.1002/mrd.21352;
RA Takiguchi H., Murayama E., Kaneko T., Kurio H., Toshimori K., Iida H.;
RT "Characterization and subcellular localization of Tektin 3 in rat
RT spermatozoa.";
RL Mol. Reprod. Dev. 78:611-620(2011).
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 (By similarity).
CC {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q6X6Z7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:A6H782}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:19423663, ECO:0000269|PubMed:21744413}. Cytoplasmic
CC vesicle, secretory vesicle, acrosome outer membrane
CC {ECO:0000269|PubMed:21744413}; Peripheral membrane protein
CC {ECO:0000305}. Note=In the sperm flagellum, localizes to the
CC periaxonemal region where it associates with the mitochondrial sheath
CC and outer dense fibers (PubMed:21744413). Not detected in the central
CC axonemal region of the flagellum (PubMed:21744413). Associates with the
CC acrosome membrane in the equatorial segment of the sperm head
CC (PubMed:21744413). Also detected just below the plasma membrane in the
CC post-acrosomal region where it might localize to the postacrosomal
CC dense lamina (By similarity). However, other studies report little or
CC no expression in the postacrosomal region (PubMed:21744413).
CC Translocates from the postacrosomal region to the equatorial segment
CC after sperm activation (By similarity). Retained in the postacromal
CC region, but not the equatorial segment, following the acrosome reaction
CC (By similarity). Some studies report strong expression in the anterior
CC cap region (By similarity). However, other studies report little or no
CC expression in the acrosomal cap (By similarity).
CC {ECO:0000250|UniProtKB:A6H782, ECO:0000269|PubMed:21744413}.
CC -!- TISSUE SPECIFICITY: Expressed in epididymal sperm (at protein level).
CC {ECO:0000269|PubMed:19423663, ECO:0000269|PubMed:21744413}.
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 -!- SIMILARITY: Belongs to the tektin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC097398; AAH97398.1; -; mRNA.
DR RefSeq; NP_001019910.1; NM_001024739.1.
DR AlphaFoldDB; Q4V8G8; -.
DR SMR; Q4V8G8; -.
DR STRING; 10116.ENSRNOP00000031637; -.
DR GlyGen; Q4V8G8; 6 sites.
DR iPTMnet; Q4V8G8; -.
DR PhosphoSitePlus; Q4V8G8; -.
DR PaxDb; Q4V8G8; -.
DR Ensembl; ENSRNOT00000038276; ENSRNOP00000031637; ENSRNOG00000027212.
DR GeneID; 287392; -.
DR KEGG; rno:287392; -.
DR UCSC; RGD:1310582; rat.
DR CTD; 64518; -.
DR RGD; 1310582; Tekt3.
DR eggNOG; KOG2685; Eukaryota.
DR GeneTree; ENSGT00950000182894; -.
DR HOGENOM; CLU_033588_2_1_1; -.
DR InParanoid; Q4V8G8; -.
DR OMA; QRIDDRC; -.
DR OrthoDB; 581072at2759; -.
DR PhylomeDB; Q4V8G8; -.
DR TreeFam; TF320754; -.
DR PRO; PR:Q4V8G8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000027212; Expressed in testis and 8 other tissues.
DR Genevisible; Q4V8G8; RN.
DR GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; IDA:UniProtKB.
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:CAFA.
DR GO; GO:0060378; P:regulation of brood size; ISS:CAFA.
DR InterPro; IPR000435; Tektin.
DR PANTHER; PTHR19960; PTHR19960; 1.
DR PRINTS; PR00511; TEKTIN.
PE 1: Evidence at protein 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_0000380247"
FT COILED 419..456
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 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; 56416 MW; 4BD58229103BE8F1 CRC64;
MEPLGSTLTA TYAHPQPAAT NFLPAIGTLT SSYRNRFPHR NLTHSLSLPW RPSTYYKTAY
NYPTLAPLSS TSQSVCESTM LPFVSNRTTL FTRYTPDDWY RSTLVGFQES NCSRHNSERL
RVDTSRLIQD KYQQIRKTQA DSTQNLGERV NDIAFWKSEI IHELDEMIGE TNALTDIKRR
LERGLIETDA PLQVARECLF HREKRMGIDL VHDEAEKELL TEVETVLCCQ ERMRRHLDKA
IAQLASDRSA QHELEKDLSD KQAALRIDDK CKHLRNTSQG VSYFRGVENV DATVSVPESW
AKFTDDNVLR SQSERAASAK LREDTENLLI VIANEMWNQF NKVNVAFTNR IAETVDAKNK
IHIHLSKTLQ EIFQTEMAIE SIRKAIKEKS AFLKVAQTRL DERTRRPNIE LCRDIAQLRL
VNEVYEVDET IQTLQQRLRD SEDTLQSLAH TKATLEHDLA VKANTLYIDQ EKCMSMRNSY
PSTLRLVGFC
