TEKT3_HUMAN
ID TEKT3_HUMAN Reviewed; 490 AA.
AC Q9BXF9; B2RAS7; D3DTT0; Q8N5R5; Q96M48;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tektin-3;
GN Name=TEKT3;
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].
RA Inoue K., Dewar K., Katsanis N., Reiter L.T., Lander E.S., Devor K.L.,
RA Wyman D.W., Lupski J.R., Birren B.;
RT "The 1,421,129 bp CMT1A duplication/HNPP deletion genomic region reveals
RT unique genome architectural features and provides insights into the recent
RT evolution of new genes.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-282.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-282.
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 [4]
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. 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 -!- INTERACTION:
CC Q9BXF9; Q96IF1: AJUBA; NbExp=3; IntAct=EBI-8644516, EBI-949782;
CC Q9BXF9; Q03989: ARID5A; NbExp=3; IntAct=EBI-8644516, EBI-948603;
CC Q9BXF9; Q86U10: ASPG; NbExp=3; IntAct=EBI-8644516, EBI-19946665;
CC Q9BXF9; Q86V38: ATN1; NbExp=3; IntAct=EBI-8644516, EBI-11954292;
CC Q9BXF9; Q13137: CALCOCO2; NbExp=5; IntAct=EBI-8644516, EBI-739580;
CC Q9BXF9; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-8644516, EBI-743033;
CC Q9BXF9; Q8WTU0: DDI1; NbExp=3; IntAct=EBI-8644516, EBI-748248;
CC Q9BXF9; Q9H8Y8: GORASP2; NbExp=4; IntAct=EBI-8644516, EBI-739467;
CC Q9BXF9; P31943: HNRNPH1; NbExp=3; IntAct=EBI-8644516, EBI-351590;
CC Q9BXF9; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-8644516, EBI-747204;
CC Q9BXF9; Q1MX18: INSC; NbExp=5; IntAct=EBI-8644516, EBI-12081118;
CC Q9BXF9; O76011: KRT34; NbExp=3; IntAct=EBI-8644516, EBI-1047093;
CC Q9BXF9; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-8644516, EBI-11992140;
CC Q9BXF9; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-8644516, EBI-1048945;
CC Q9BXF9; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-8644516, EBI-3957672;
CC Q9BXF9; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-8644516, EBI-9996449;
CC Q9BXF9; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-8644516, EBI-12111050;
CC Q9BXF9; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-8644516, EBI-11962084;
CC Q9BXF9; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-8644516, EBI-10261141;
CC Q9BXF9; Q14847-2: LASP1; NbExp=3; IntAct=EBI-8644516, EBI-9088686;
CC Q9BXF9; P25791-3: LMO2; NbExp=3; IntAct=EBI-8644516, EBI-11959475;
CC Q9BXF9; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-8644516, EBI-8487781;
CC Q9BXF9; O43482: OIP5; NbExp=5; IntAct=EBI-8644516, EBI-536879;
CC Q9BXF9; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-8644516, EBI-2876622;
CC Q9BXF9; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-8644516, EBI-949255;
CC Q9BXF9; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-8644516, EBI-744023;
CC Q9BXF9; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-8644516, EBI-746118;
CC Q9BXF9; Q99932-2: SPAG8; NbExp=4; IntAct=EBI-8644516, EBI-11959123;
CC Q9BXF9; Q8NA69: TEX45; NbExp=3; IntAct=EBI-8644516, EBI-12021638;
CC Q9BXF9; Q63HR2: TNS2; NbExp=3; IntAct=EBI-8644516, EBI-949753;
CC Q9BXF9; Q12933: TRAF2; NbExp=6; IntAct=EBI-8644516, EBI-355744;
CC Q9BXF9; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-8644516, EBI-492476;
CC Q9BXF9; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-8644516, EBI-12040603;
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 -!- 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}.
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DR EMBL; AF334676; AAK15340.1; -; mRNA.
DR EMBL; AK057390; BAB71464.1; -; mRNA.
DR EMBL; AK314327; BAG36974.1; -; mRNA.
DR EMBL; CH471108; EAW89942.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW89943.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW89944.1; -; Genomic_DNA.
DR EMBL; BC031688; AAH31688.1; -; mRNA.
DR CCDS; CCDS11169.1; -.
DR RefSeq; NP_114104.1; NM_031898.2.
DR RefSeq; XP_011522290.1; XM_011523988.2.
DR RefSeq; XP_011522291.1; XM_011523989.1.
DR RefSeq; XP_016880443.1; XM_017024954.1.
DR AlphaFoldDB; Q9BXF9; -.
DR SMR; Q9BXF9; -.
DR BioGRID; 122203; 39.
DR IntAct; Q9BXF9; 39.
DR MINT; Q9BXF9; -.
DR STRING; 9606.ENSP00000379263; -.
DR GlyGen; Q9BXF9; 9 sites.
DR iPTMnet; Q9BXF9; -.
DR PhosphoSitePlus; Q9BXF9; -.
DR BioMuta; TEKT3; -.
DR DMDM; 25009463; -.
DR MassIVE; Q9BXF9; -.
DR PaxDb; Q9BXF9; -.
DR PeptideAtlas; Q9BXF9; -.
DR PRIDE; Q9BXF9; -.
DR ProteomicsDB; 79421; -.
DR Antibodypedia; 25125; 144 antibodies from 21 providers.
DR DNASU; 64518; -.
DR Ensembl; ENST00000338696.6; ENSP00000343995.2; ENSG00000125409.13.
DR Ensembl; ENST00000395930.6; ENSP00000379263.1; ENSG00000125409.13.
DR GeneID; 64518; -.
DR KEGG; hsa:64518; -.
DR MANE-Select; ENST00000395930.6; ENSP00000379263.1; NM_031898.3; NP_114104.1.
DR UCSC; uc002gon.4; human.
DR CTD; 64518; -.
DR DisGeNET; 64518; -.
DR GeneCards; TEKT3; -.
DR HGNC; HGNC:14293; TEKT3.
DR HPA; ENSG00000125409; Tissue enriched (testis).
DR MIM; 612683; gene.
DR neXtProt; NX_Q9BXF9; -.
DR OpenTargets; ENSG00000125409; -.
DR PharmGKB; PA37865; -.
DR VEuPathDB; HostDB:ENSG00000125409; -.
DR eggNOG; KOG2685; Eukaryota.
DR GeneTree; ENSGT00950000182894; -.
DR HOGENOM; CLU_033588_2_1_1; -.
DR InParanoid; Q9BXF9; -.
DR OMA; QRIDDRC; -.
DR OrthoDB; 581072at2759; -.
DR PhylomeDB; Q9BXF9; -.
DR TreeFam; TF320754; -.
DR PathwayCommons; Q9BXF9; -.
DR SignaLink; Q9BXF9; -.
DR BioGRID-ORCS; 64518; 7 hits in 1068 CRISPR screens.
DR GenomeRNAi; 64518; -.
DR Pharos; Q9BXF9; Tbio.
DR PRO; PR:Q9BXF9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BXF9; protein.
DR Bgee; ENSG00000125409; Expressed in left testis and 95 other tissues.
DR ExpressionAtlas; Q9BXF9; baseline and differential.
DR Genevisible; Q9BXF9; HS.
DR GO; GO:0002080; C:acrosomal membrane; ISS:CAFA.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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 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_0000184568"
FT COILED 424..451
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 10
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"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 3
FT /note="R -> H (in dbSNP:rs7226363)"
FT /id="VAR_053721"
FT VARIANT 282
FT /note="G -> A (in dbSNP:rs230898)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT /id="VAR_024658"
FT VARIANT 296
FT /note="V -> A (in dbSNP:rs6502446)"
FT /id="VAR_024659"
FT VARIANT 410
FT /note="E -> D (in dbSNP:rs35855709)"
FT /id="VAR_034550"
FT CONFLICT 268
FT /note="D -> N (in Ref. 4; AAH31688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 56636 MW; F385314A08651C69 CRC64;
MERVGCTLTT TYAHPRPTPT NFLPAISTMA SSYRDRFPHS NLTHSLSLPW RPSTYYKVAS
NSPSVAPYCT RSQRVSENTM LPFVSNRTTF FTRYTPDDWY RSNLTNYQES NTSRHNSEKL
RVDTSRLIQD KYQQTRKTQA DTTQNLGERV NDIGFWKSEI IHELDEMIGE TNALTDVKKR
LERALMETEA PLQVARECLF HREKRMGIDL VHDEVEAQLL TEVDTILCCQ ERMKLHLDKA
IAQLAANRAS QHELEKDLSD KQTAYRIDDK CHHLRNTSDG VGYFRGVERV DATVSVPESW
AKFTDDNILR SQSERAASAK LRDDIENLLV VTANEMWNQF NKVNLSFTNR IAETADAKNK
IQTHLAKTLQ EIFQTEMTIE SIKKAIKDKT AFLKVAQTRL DERTRRPNIE LCRDMAQLRL
VNEVHEVDDT IQTLQQRLRD AEDTLQSLVH IKATLEYDLA VKANSLYIDQ EKCMSMRKSY
PNTLRLVGFC
