SMK_RAT
ID SMK_RAT Reviewed; 654 AA.
AC A1A5Q6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Sperm motility kinase;
DE EC=2.7.11.1;
GN Name=Smok;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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: May play a role in sperm motility, especially in the
CC regulation of flagellar function. {ECO:0000250}.
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. Smok subfamily. {ECO:0000305}.
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DR EMBL; BC128761; AAI28762.1; -; mRNA.
DR RefSeq; NP_001094414.1; NM_001100944.1.
DR RefSeq; XP_017443089.1; XM_017587600.1.
DR RefSeq; XP_017443090.1; XM_017587601.1.
DR RefSeq; XP_017455531.1; XM_017600042.1.
DR AlphaFoldDB; A1A5Q6; -.
DR SMR; A1A5Q6; -.
DR STRING; 10116.ENSRNOP00000033067; -.
DR PaxDb; A1A5Q6; -.
DR PeptideAtlas; A1A5Q6; -.
DR PRIDE; A1A5Q6; -.
DR Ensembl; ENSRNOT00000039592; ENSRNOP00000033067; ENSRNOG00000022181.
DR GeneID; 290818; -.
DR KEGG; rno:290818; -.
DR UCSC; RGD:1562638; rat.
DR CTD; 290818; -.
DR RGD; 1562638; RGD1562638.
DR eggNOG; KOG0586; Eukaryota.
DR GeneTree; ENSGT00940000160886; -.
DR HOGENOM; CLU_000288_157_6_1; -.
DR InParanoid; A1A5Q6; -.
DR OMA; FRRRVWK; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; A1A5Q6; -.
DR PRO; PR:A1A5Q6; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000022181; Expressed in testis.
DR GO; GO:0005524; F:ATP 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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..654
FT /note="Sperm motility kinase"
FT /id="PRO_0000307878"
FT DOMAIN 24..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 289..329
FT /note="UBA"
FT REGION 336..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 654 AA; 73847 MW; BDEACD7B3484558B CRC64;
MKRWQVCQDL RSSPFQEDAL TDHYRILASL GQGGFGEVKL ASHLLTQTKV AIKVLPKSNK
NLLLKSEIEI MKSLDHPHII KLLHIIDTNE NIFIVLEHAV GGELLTRIED FGYLPEEECN
RLFRQMVLAL QYCHQRGIIH RDIKPENILL DHKGNVKLSD FGLSTKIVMG QKLTTLCGTL
PYCAPELFNL NGYDGQAIDV WSLGVVLYYM ATGCLPFQGF TYQAIKQKIL SGRYSVNFRL
SPDLWDVIAK LLTVNPRERP RVHEILRFNW LKNENEVSPS SLGGNTDSHP DPTILVMMGD
MGYEQGQIRE SLRERKFDQV MATYLMLREK ACSEDKSIKT PHPTQCAQTL KSTGSTTEKQ
TTLRRGSSLP TLTTFYLPSK LESLNKEKRT TMRHTMPPNL NCFNKSESLN KGRRTIVSHT
ISPTLNCFNK SESLNKGKRT IVRHTMPPKK TSPVRRICPR LHKSFGMGSA SEDSSKRNSS
DPSLTIFSSQ SFMSAFKYGS TYSKRKAFLQ CILHYHASQE EDQYKTTIIP SGKLNTTVPP
NSLQEDQPTG HLHNVLTAGA VDNRNLQEKS PPFSTTATKG EGPAIKERES IPSSPRAPRE
QFRGRSQTPP RAPFRRRVWK TLKSGFLKGL GSLCCCLPIQ KKVHPASNRV PPMK
