TSSK1_BOVIN
ID TSSK1_BOVIN Reviewed; 367 AA.
AC Q3SZW1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Testis-specific serine/threonine-protein kinase 1;
DE Short=TSK-1;
DE Short=TSK1;
DE Short=TSSK-1;
DE Short=Testis-specific kinase 1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q61241};
GN Name=TSSK1B; Synonyms=TSSK1;
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 MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Testis-specific serine/threonine-protein kinase required
CC during spermatid development. Phosphorylates 'Ser-288' of TSKS.
CC Involved in the late stages of spermatogenesis, during the
CC reconstruction of the cytoplasm. During spermatogenesis, required for
CC the transformation of a ring-shaped structure around the base of the
CC flagellum originating from the chromatoid body (By similarity).
CC {ECO:0000250|UniProtKB:Q61241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q61241};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q61241};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q61241};
CC -!- SUBUNIT: Interacts with TSSK2. Interacts with HSP90; this interaction
CC stabilizes TSSK1. {ECO:0000250|UniProtKB:Q61241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC secretory vesicle, acrosome {ECO:0000250}. Cell projection, cilium,
CC flagellum {ECO:0000250}. Note=In spermatozoa, present in the sperm head
CC and in the flagellum. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXA7}.
CC -!- PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination
CC and degradation. {ECO:0000250|UniProtKB:Q61241}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BC102681; AAI02682.1; -; mRNA.
DR RefSeq; NP_001077179.1; NM_001083710.2.
DR AlphaFoldDB; Q3SZW1; -.
DR SMR; Q3SZW1; -.
DR STRING; 9913.ENSBTAP00000056044; -.
DR PaxDb; Q3SZW1; -.
DR GeneID; 529193; -.
DR KEGG; bta:529193; -.
DR CTD; 83942; -.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q3SZW1; -.
DR OrthoDB; 947464at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Differentiation; Flagellum; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Spermatogenesis; Transferase;
KW Ubl conjugation.
FT CHAIN 1..367
FT /note="Testis-specific serine/threonine-protein kinase 1"
FT /id="PRO_0000248286"
FT DOMAIN 12..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 282..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXA7"
SQ SEQUENCE 367 AA; 41569 MW; 6628B66519D46076 CRC64;
MDDAAVLKRR GYIMGINLGE GSYAKVKSAY SERLKFNVAV KIIDRKKAPT DFLEKFLPRE
IEILAMLNHR SIIKTYEIFE TSDGKVYIVM ELGVQGDLLE FIKTRGALQE DDARKKFHQL
SSAIKYCHDL DVVHRDLKCE NLLLDKDFNI KLSDFGFSKR CLRDDSGRLT LSKTFCGSAA
YAAPEVLQGI PYQPKVYDIW SLGVILYIMV CGSMPYDDSN IKKMLRIQKE HRVNFPRSKH
LTGECKDLIY RMLQPDVTRR LHIDEILSHC WVQPKARGLS SAAVNKEGES SRAAEPPWTP
EPSSDKKSAT KLEPREEVRP EPRAEPSPEE EMATVQVSRQ SEAVGLPSEQ PSKTEEGAPP
QPSETHA
