KIN1_SCHPO
ID KIN1_SCHPO Reviewed; 891 AA.
AC P22987; O74392;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protein kinase kin1;
DE EC=2.7.11.1;
GN Name=kin1; ORFNames=SPBC4F6.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2236039; DOI=10.1073/pnas.87.21.8272;
RA Levin D.E., Bishop J.M.;
RT "A putative protein kinase gene (kin1+) is important for growth polarity in
RT Schizosaccharomyces pombe.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8272-8276(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14596912; DOI=10.1016/s0014-5793(03)01080-9;
RA Drewes G., Nurse P.;
RT "The protein kinase kin1, the fission yeast orthologue of mammalian
RT MARK/PAR-1, localises to new cell ends after mitosis and is important for
RT bipolar growth.";
RL FEBS Lett. 554:45-49(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-528; SER-535 AND SER-536, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in establishing the characteristic rod cell shape.
CC Important for cell polarity and is involved in directing growth to the
CC cell ends. {ECO:0000269|PubMed:14596912}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14596912}.
CC Note=Localized to the cell tips except during mitosis.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M64999; AAA63577.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20726.1; -; Genomic_DNA.
DR PIR; A38903; A38903.
DR PIR; T40503; T40503.
DR RefSeq; NP_596106.1; NM_001022023.2.
DR AlphaFoldDB; P22987; -.
DR SMR; P22987; -.
DR BioGRID; 277311; 473.
DR STRING; 4896.SPBC4F6.06.1; -.
DR iPTMnet; P22987; -.
DR MaxQB; P22987; -.
DR PaxDb; P22987; -.
DR PRIDE; P22987; -.
DR EnsemblFungi; SPBC4F6.06.1; SPBC4F6.06.1:pep; SPBC4F6.06.
DR GeneID; 2540792; -.
DR KEGG; spo:SPBC4F6.06; -.
DR PomBase; SPBC4F6.06; kin1.
DR VEuPathDB; FungiDB:SPBC4F6.06; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_002664_0_2_1; -.
DR InParanoid; P22987; -.
DR OMA; MFDFYKR; -.
DR PhylomeDB; P22987; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P22987; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990873; C:intrinsic component of plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0032178; C:medial membrane band; IDA:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; TAS:PomBase.
DR GO; GO:0035841; C:new growing cell tip; IDA:PomBase.
DR GO; GO:0035839; C:non-growing cell tip; IDA:PomBase.
DR GO; GO:0035842; C:old cell tip after activation of bipolar cell growth; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; EXP:PomBase.
DR GO; GO:0051523; P:cell growth mode switching, monopolar to bipolar; IMP:PomBase.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1902408; P:mitotic cytokinesis, site selection; IMP:PomBase.
DR GO; GO:0007009; P:plasma membrane organization; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..891
FT /note="Protein kinase kin1"
FT /id="PRO_0000086130"
FT DOMAIN 125..395
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 842..891
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 65..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 131..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 528
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 141
FT /note="V -> D (in Ref. 1; AAA63577)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="V -> E (in Ref. 1; AAA63577)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="I -> N (in Ref. 1; AAA63577)"
FT /evidence="ECO:0000305"
FT CONFLICT 777..778
FT /note="IR -> ML (in Ref. 1; AAA63577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 891 AA; 98749 MW; 89D9BB6D825C0358 CRC64;
MEYRTNNVPV GNETKSAALN ALPKIKISDS PNRHHNLVDA FMQSPSYSTQ PKSAVEPLGL
SFSPGYISPS SQSPHHGPVR SPSSRKPLPA SPSRTRDHSL RVPVSGHSYS ADEKPRERRK
VIGNYVLGKT IGAGSMGKVK VAHHLKTGEQ FAIKIVTRLH PDITKAKAAA SAEATKAAQS
EKNKEIRTVR EAALSTLLRH PYICEARDVY ITNSHYYMVF EFVDGGQMLD YIISHGKLKE
KQARKFVRQI GSALSYLHQN SVVHRDLKIE NILISKTGDI KIIDFGLSNL YRRQSRLRTF
CGSLYFAAPE LLNAQPYIGP EVDVWSFGIV LYVLVCGKVP FDDQNMSALH AKIKKGTVEY
PSYLSSDCKG LLSRMLVTDP LKRATLEEVL NHPWMIRNYE GPPASFAPER SPITLPLDPE
IIREMNGFDF GPPEKIVREL TKVISSEAYQ SLAKTGFYSG PNSADKKKSF FEFRIRHAAH
DIENPILPSL SMNTDIYDAF HPLISIYYLV SERRVYEKGG NWNRIAKTPV SSVPSSPVQP
TSYNRTLPPM PEVVAYKGDE ESPRVSRNTS LARRKPLPDT ESHSPSPSAT SSIKKNPSSI
FRRFSSRRKQ NKSSTSTLQI SAPLETSQSP PTPRTKPSHK PPVSYKNKLV TQSAIGRSTS
VREGRYAGIS SQMDSLNMDS TGPSASNMAN APPSVRNNRV LNPRGASLGH GRMSTSTTNR
QKQILNETMG NPVDKNSTSP SKSTDKLDPI KPVFLKGLFS VSTTSTKSTE SIQRDLIRVM
GMLDIEYKEI KGGYACLYKP QGIRTPTKST SVHTRRKPSY GSNSTTDSYG SVPDTVPLDD
NGESPASNLA FEIYIVKVPI LSLRGVSFHR ISGNSWQYKT LASRILNELK L
