TEKT2_HUMAN
ID TEKT2_HUMAN Reviewed; 430 AA.
AC Q9UIF3; A6NIS6; O60638;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tektin-2;
DE AltName: Full=Tektin-t;
DE AltName: Full=Testicular tektin;
DE AltName: Full=Testicular tektin B1-like protein;
DE Short=TEKTB1;
DE Short=Tektin-B1;
GN Name=TEKT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 188-195; 259-266; 322-331;
RP 356-368 AND 404-413, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=11751288; DOI=10.1095/biolreprod66.1.241;
RA Wolkowicz M.J., Naaby-Hansen S., Gamble A.R., Reddi P.P., Flickinger C.J.,
RA Herr J.C.;
RT "Tektin B1 demonstrates flagellar localization in human sperm.";
RL Biol. Reprod. 66:241-250(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=12029069; DOI=10.1093/molehr/8.6.525;
RA Iguchi N., Tanaka H., Nakamura Y., Nozaki M., Fujiwara T., Nishimune Y.;
RT "Cloning and characterization of the human tektin-t gene.";
RL Mol. Hum. Reprod. 8:525-530(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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: Expressed at high levels in testis, trachea and
CC fetal lung, and at lower levels in ovary, pituitary, adult lung, fetal
CC brain and fetal kidney. {ECO:0000269|PubMed:11751288}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q1W6C3}.
CC -!- SIMILARITY: Belongs to the tektin family. {ECO:0000305}.
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DR EMBL; AF054910; AAC09343.1; -; mRNA.
DR EMBL; AB033823; BAA89350.1; -; mRNA.
DR EMBL; AL138787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07392.1; -; Genomic_DNA.
DR EMBL; BC035620; AAH35620.1; -; mRNA.
DR CCDS; CCDS401.1; -.
DR RefSeq; NP_055281.2; NM_014466.2.
DR RefSeq; XP_005270810.1; XM_005270753.2.
DR RefSeq; XP_011539560.1; XM_011541258.2.
DR RefSeq; XP_016856544.1; XM_017001055.1.
DR AlphaFoldDB; Q9UIF3; -.
DR SMR; Q9UIF3; -.
DR BioGRID; 118109; 22.
DR IntAct; Q9UIF3; 14.
DR STRING; 9606.ENSP00000207457; -.
DR iPTMnet; Q9UIF3; -.
DR PhosphoSitePlus; Q9UIF3; -.
DR BioMuta; TEKT2; -.
DR DMDM; 25009466; -.
DR MassIVE; Q9UIF3; -.
DR PaxDb; Q9UIF3; -.
DR PeptideAtlas; Q9UIF3; -.
DR PRIDE; Q9UIF3; -.
DR ProteomicsDB; 84499; -.
DR Antibodypedia; 17404; 146 antibodies from 23 providers.
DR DNASU; 27285; -.
DR Ensembl; ENST00000207457.8; ENSP00000207457.3; ENSG00000092850.12.
DR GeneID; 27285; -.
DR KEGG; hsa:27285; -.
DR MANE-Select; ENST00000207457.8; ENSP00000207457.3; NM_014466.3; NP_055281.2.
DR UCSC; uc001bzr.3; human.
DR CTD; 27285; -.
DR DisGeNET; 27285; -.
DR GeneCards; TEKT2; -.
DR HGNC; HGNC:11725; TEKT2.
DR HPA; ENSG00000092850; Group enriched (fallopian tube, testis).
DR MIM; 608953; gene.
DR neXtProt; NX_Q9UIF3; -.
DR OpenTargets; ENSG00000092850; -.
DR PharmGKB; PA36442; -.
DR VEuPathDB; HostDB:ENSG00000092850; -.
DR eggNOG; KOG2685; Eukaryota.
DR GeneTree; ENSGT00950000182894; -.
DR HOGENOM; CLU_033588_0_0_1; -.
DR InParanoid; Q9UIF3; -.
DR OMA; FDHRGKM; -.
DR OrthoDB; 581072at2759; -.
DR PhylomeDB; Q9UIF3; -.
DR TreeFam; TF320754; -.
DR PathwayCommons; Q9UIF3; -.
DR SignaLink; Q9UIF3; -.
DR SIGNOR; Q9UIF3; -.
DR BioGRID-ORCS; 27285; 60 hits in 1070 CRISPR screens.
DR GenomeRNAi; 27285; -.
DR Pharos; Q9UIF3; Tbio.
DR PRO; PR:Q9UIF3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UIF3; protein.
DR Bgee; ENSG00000092850; Expressed in right uterine tube and 89 other tissues.
DR ExpressionAtlas; Q9UIF3; baseline and differential.
DR Genevisible; Q9UIF3; HS.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0036159; P:inner dynein arm assembly; IEA:Ensembl.
DR InterPro; IPR000435; Tektin.
DR PANTHER; PTHR19960; PTHR19960; 1.
DR PRINTS; PR00511; TEKTIN.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Flagellum; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..430
FT /note="Tektin-2"
FT /id="PRO_0000184565"
FT COILED 80..162
FT /evidence="ECO:0000255"
FT COILED 225..382
FT /evidence="ECO:0000255"
FT VARIANT 46
FT /note="R -> C (in dbSNP:rs12043423)"
FT /id="VAR_034549"
FT VARIANT 114
FT /note="I -> T (in dbSNP:rs419653)"
FT /id="VAR_053720"
FT CONFLICT 329
FT /note="L -> F (in Ref. 1; AAC09343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 49672 MW; BD7600E20624DD25 CRC64;
MATLSVKPSR RFQLPDWHTN SYLLSTNAQL QRDASHQIRQ EARVLRNETN NQTIWDEHDN
RTRLVERIDT VNRWKEMLDK CLTDLDAEID ALTQMKESAE QNLQAKNLPL DVAIECLTLR
ESRRDIDVVK DPVEDELHKE VEVIEATKKA LQQKVSQAFE QLCLLQEVQQ QLNSDHRGKM
ETLEIDRGCL SLNLRSPNIS LKVDPTRVPD GSTTLQQWDD FSRFNKDRAE AEMKAATELR
EATALTIAET NNELEAQRVA TEFAFRKRLR EMEKVYSELK WQEKNTLEEI AELQEDIRHL
EEDLRTKLLS LKLSHTRLEA RTYRPNVELC RDQAQYGLTD EVHQLEATIA ALKQKLAQAQ
DALDALCKHL ARLQADIACK ANSMLLDTKC MDTRRKLTVP AERFVPEVDT FTRTTNSTLS
PLKSCQLELA
