TEX14_BOVIN
ID TEX14_BOVIN Reviewed; 1493 AA.
AC F1MJR8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Inactive serine/threonine-protein kinase TEX14;
DE AltName: Full=Testis-expressed sequence 14;
DE AltName: Full=Testis-expressed sequence 14 protein;
GN Name=TEX14;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Required both for the formation of intercellular bridges
CC during meiosis and for kinetochore-microtubule attachment during
CC mitosis. Intercellular bridges are evolutionarily conserved structures
CC that connect differentiating germ cells and are required for
CC spermatogenesis and male fertility. Acts by promoting the conversion of
CC midbodies into intercellular bridges via its interaction with CEP55:
CC interaction with CEP55 inhibits the interaction between CEP55 and
CC PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to
CC transform midbodies into intercellular bridges. Also plays a role
CC during mitosis: recruited to kinetochores by PLK1 during early mitosis
CC and regulates the maturation of the outer kinetochores and microtubule
CC attachment. Has no protein kinase activity in vitro (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KIF23 and RBM44. Interacts with CEP55;
CC inhibiting interaction between CEP55 and PDCD6IP/ALIX and TSG101 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Midbody {ECO:0000250}.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Note=Detected in the
CC intercellular bridges that connect male germ cell daughter cells after
CC cell division. {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DOMAIN: The GPPX3Y motif mediates interaction with CEP55.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Thr residues by CDK1 during early phases of
CC mitosis, promoting the interaction with PLK1 and recruitment to
CC kinetochores. Phosphorylated on Ser-430 by PLK1 during late
CC prometaphase promotes the rapid depletion from kinetochores and its
CC subsequent degradation by the APC/C complex.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: In contrast to protein kinases, Ser-369 is present instead of
CC the conserved Asp which is expected to be an active site residue.
CC {ECO:0000305}.
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DR EMBL; DAAA02048320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02048321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02048322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02048323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179497.1; NM_001192568.1.
DR AlphaFoldDB; F1MJR8; -.
DR SMR; F1MJR8; -.
DR STRING; 9913.ENSBTAP00000013424; -.
DR PaxDb; F1MJR8; -.
DR PRIDE; F1MJR8; -.
DR Ensembl; ENSBTAT00000013424; ENSBTAP00000013424; ENSBTAG00000010167.
DR GeneID; 522810; -.
DR KEGG; bta:522810; -.
DR CTD; 56155; -.
DR VEuPathDB; HostDB:ENSBTAG00000010167; -.
DR VGNC; VGNC:35762; TEX14.
DR eggNOG; ENOG502QSZN; Eukaryota.
DR GeneTree; ENSGT00390000015123; -.
DR HOGENOM; CLU_004733_0_0_1; -.
DR InParanoid; F1MJR8; -.
DR OMA; LCFQFYL; -.
DR OrthoDB; 92703at2759; -.
DR TreeFam; TF328704; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000010167; Expressed in spermatocyte and 83 other tissues.
DR ExpressionAtlas; F1MJR8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0043063; P:intercellular bridge organization; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR039339; Tex14.
DR PANTHER; PTHR23060; PTHR23060; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ANK repeat; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Kinetochore; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1493
FT /note="Inactive serine/threonine-protein kinase TEX14"
FT /id="PRO_0000417521"
FT REPEAT 27..54
FT /note="ANK 1"
FT REPEAT 55..84
FT /note="ANK 2"
FT REPEAT 88..117
FT /note="ANK 3"
FT DOMAIN 198..511
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 559..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 789..795
FT /note="GPPX3Y"
FT MOTIF 846..854
FT /note="D-box"
FT COMPBIAS 851..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 430
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
SQ SEQUENCE 1493 AA; 165254 MW; 0625799807E402D9 CRC64;
MSRAVHLPVP CPVQLGSLRN DSLEAQLHEY VKQGNYVKVK RILKKGIYVD AVNSLGQTAL
FIAALLGLTK LVDVLVDYGA DPNHRCFDGS TPVHAAAFSG NQWILSKLLD AGGDLRLHDE
KGRNPQTWAL AAGKERSTVM VEFMQRCAAH MQAIIQGFSD LLKKIDSPQR LISGVPRFGG
LMQGNPNGSP NRPPKAGVIS AQNIYSFGFG KFYLTGGTQL AYLGSLPVIG EKEVIQADDE
PTFSFFSGPY MVMTNLVWNG SRVTVKELHL STHPHCSRLR MADLLIAEQE HSSKLRHPHV
LQLMAVCLSP DLEKTRLVYE RVTVGTLFSV LHERRAQFPV LHMEVIVHLL LQISDALRYL
HSRGFIHRSL SSYAIHIVST GEARLTNLEY MMESQDGGAH RGLTRVPLPT QLYNWAAPEV
IIQKAATVKS DIYSFSVIVQ EILTDNIPWD GLDGSVIKET IVLGNYLEAD VRLPKPYYDI
VKSGLQVKQK DRTMNLQDIR YIMKNDLKDF IGAQRTQPTE SPRVQRYEFH PDVNVCLGLT
SEHPKETPNL EIKELKETGS QFHSPRGHSS PTGKATPEPP VPDVSPVAQQ THRQDAASPA
CSVAEEARNP SPDQTSLCSF EINEIYSGCL DTADDPEEEC PGTGSSLEGA IPNQTDELKS
MEEELEKMER EVCCSCDEDE SSSDADTELS CEDWEWQNDA LCSPSRPEPA RGAKGATNNR
SMTEEYISKC VLNLKISQTL IHQNADLLRN VQQKIEKLEM IQKEQAERRS LWASSREFAG
IHDSPSALGP PASSYLPPVV QRPGDQQLDP GGSGLTLARS PRTLPTLCGP GKQSRGEQFQ
PTHGAKASLE RDRNQNTSSQ GRPRESSPQS KTTQLSSALL TVPSHPQGSP TSSKPGQDST
RISMQSVSSE IYNAKSRNNK DDGEIHLKWK TEVKEMAAKA ATGQLTVPPW HPRSGVALDS
EAENEPDPLP QLPIRVSEHM DWQQAADYLK KSDEPGGNDK CGQTDSSDQR GRQSGPQRFT
SIRHLPPRED EQPEHSEVFQ ANSDASVAVE KSYSGQSAQS TCSPESSEDT EDMTDEFLTP
DHEYFYSSIA QENLALETSS PIDEDFEGIQ HACARPQASG EEKFQMRKNL GKNSEILTKS
QFQPIRSPEG EQDETLKEPP KEVKEKDISL TDIQDLSSIS CEHDGSFKEV SCKTPKINHA
PTSVSTPLSP GSLSSVASQY KDCLESIPFQ DTKTGSTSCG TSQESTQTLS DKFTSVREKA
KSLDSLLTSS EVLPARLTNL KRLPAFTGAG SSSIAKAPDT SRCATQRRSL PKELVEAISQ
HHIDELPPPS QELLDEIEHL KGQQVSSTAL DENTASRPGS TENDQRHLEE QETHSNKEDS
SMLWTKETQD LEEDTERAHS TLDEDLERWL QPPEDSTQLP DLPKGPAREA SSKDQEVGEK
KRKGEESTKP EKRKPESFLG TSEEEELKPC FWKRLGWSEP SRIIVLDQSD LSD
