ID   TEKT2_MESAU             Reviewed;          87 AA.
AC   Q1W6C3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Tektin-2 {ECO:0000250|UniProtKB:Q922G7, ECO:0000312|EMBL:ABD91531.1};
DE   AltName: Full=Tektin-t {ECO:0000250|UniProtKB:Q922G7};
DE   AltName: Full=Testicular tektin {ECO:0000250|UniProtKB:Q922G7};
DE   Flags: Fragment;
GN   Name=TEKT2 {ECO:0000250|UniProtKB:Q922G7};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABD91531.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Testis {ECO:0000269|PubMed:19953638};
RX   PubMed=19953638; DOI=10.1002/mrd.21131;
RA   Mariappa D., Aladakatti R.H., Dasari S.K., Sreekumar A., Wolkowicz M.,
RA   van der Hoorn F., Seshagiri P.B.;
RT   "Inhibition of tyrosine phosphorylation of sperm flagellar proteins, outer
RT   dense fiber protein-2 and tektin-2, is associated with impaired motility
RT   during capacitation of hamster spermatozoa.";
RL   Mol. Reprod. Dev. 77:182-193(2010).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
CC   -!- FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated
CC       doublet microtubules (DMTs) in cilia and flagellar axoneme. Plays a key
CC       role in the assembly or attachment of the inner dynein arm to
CC       microtubules in sperm flagella and tracheal cilia. Forms filamentous
CC       polymers in the walls of ciliary and flagellar microtubules.
CC       {ECO:0000250|UniProtKB:Q922G7}.
CC   -!- SUBUNIT: May interact with CCDC172. {ECO:0000250|UniProtKB:Q922G7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q922G7}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000250|UniProtKB:Q922G7}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center {ECO:0000250|UniProtKB:Q922G7}.
CC       Note=Colocalized with CCDC172 at the perinuclear region.
CC       {ECO:0000250|UniProtKB:Q922G7}.
CC   -!- TISSUE SPECIFICITY: Detected in sperm flagella (at protein level).
CC       {ECO:0000269|PubMed:19953638}.
CC   -!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:19953638}.
CC   -!- SIMILARITY: Belongs to the tektin family. {ECO:0000255}.
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DR   EMBL; DQ431410; ABD91531.1; -; mRNA.
DR   AlphaFoldDB; Q1W6C3; -.
DR   SMR; Q1W6C3; -.
DR   STRING; 10036.XP_005084438.1; -.
DR   eggNOG; KOG2685; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IEA:InterPro.
DR   InterPro; IPR000435; Tektin.
DR   PANTHER; PTHR19960; PTHR19960; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Flagellum; Microtubule; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           <1..>87
FT                   /note="Tektin-2"
FT                   /id="PRO_0000394424"
FT   COILED          26..55
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABD91531.1"
FT   NON_TER         87
FT                   /evidence="ECO:0000312|EMBL:ABD91531.1"
SQ   SEQUENCE   87 AA;  10076 MW;  604528A6FF01ABA1 CRC64;
     LPLDVAIECL TLRESRRDID VVRDPVEEEL LKEVEVIEAT KKALQQRVSQ AFQQLCLLQE
     VRQQLCSDHR DKMESLDIDR GCLSLNL