PKD2_SCHPO
ID PKD2_SCHPO Reviewed; 710 AA.
AC Q09917;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=TRP-like ion channel pkd2;
DE AltName: Full=Polycystic kidney disease-related ion channel 2;
DE Flags: Precursor;
GN Name=pkd2; ORFNames=SPAC1F7.03;
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 [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 [2]
RP FUNCTION, INTERACTION WITH RHO1, AND SUBCELLULAR LOCATION.
RX PubMed=15537393; DOI=10.1042/bj20041710;
RA Palmer C.P., Aydar E., Djamgoz M.B.;
RT "A microbial TRP-like polycystic-kidney-disease-related ion channel gene.";
RL Biochem. J. 387:211-219(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599 AND SER-632, 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: Acts as a key signaling component in the regulation of cell
CC shape and cell wall synthesis through interaction with GTPase Rho1.
CC {ECO:0000269|PubMed:15537393}.
CC -!- SUBUNIT: Interacts with rho1. {ECO:0000269|PubMed:15537393}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15537393};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15537393}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:15537393}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:15537393}.
CC -!- SIMILARITY: Belongs to the transient receptor potential (TRP) ion
CC channel family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91950.1; -; Genomic_DNA.
DR PIR; S62575; S62575.
DR RefSeq; NP_594489.1; NM_001019918.2.
DR AlphaFoldDB; Q09917; -.
DR BioGRID; 278110; 4.
DR STRING; 4896.SPAC1F7.03.1; -.
DR TCDB; 1.A.4.9.2; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; Q09917; -.
DR PaxDb; Q09917; -.
DR PRIDE; Q09917; -.
DR EnsemblFungi; SPAC1F7.03.1; SPAC1F7.03.1:pep; SPAC1F7.03.
DR GeneID; 2541613; -.
DR KEGG; spo:SPAC1F7.03; -.
DR PomBase; SPAC1F7.03; pkd2.
DR VEuPathDB; FungiDB:SPAC1F7.03; -.
DR eggNOG; ENOG502QSVZ; Eukaryota.
DR HOGENOM; CLU_010226_1_0_1; -.
DR InParanoid; Q09917; -.
DR OMA; FLYVQFK; -.
DR PhylomeDB; Q09917; -.
DR PRO; PR:Q09917; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032154; C:cleavage furrow; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0030133; C:transport vesicle; IDA:PomBase.
DR GO; GO:0005262; F:calcium channel activity; IMP:PomBase.
DR GO; GO:0140135; F:mechanosensitive cation channel activity; ISS:PomBase.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IMP:PomBase.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:PomBase.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0061454; P:release of sequestered calcium ion into cytosol by Golgi; IGI:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR010308; TRP_C.
DR InterPro; IPR040241; TRP_Flc/Pkd2-like.
DR InterPro; IPR032800; TRP_N.
DR PANTHER; PTHR31145; PTHR31145; 1.
DR Pfam; PF06011; TRP; 1.
DR Pfam; PF14558; TRP_N; 1.
DR SMART; SM01320; TRP_N; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Golgi apparatus; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..710
FT /note="TRP-like ion channel pkd2"
FT /id="PRO_0000045821"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 689..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 710 AA; 79989 MW; 0A4D5B7371F84278 CRC64;
MRLWRSPLLL LVVVVELFSW ADALTRFISA DSLSTCMTDS QLSASKLYAS YFPDNQSVAF
DISIQSLVST NVSIDVDISA YGIEIKKVID PCDMEISGFC PMQTGNIALS GSHTLTGEAL
SILDSIPSIA YTVPDLDAVV TINIYESDTN TQLACVRTTV QNGRSVYHRA VYWVMCMVIG
IPLLIFLLIS PVLQTPALWE IVETMITLFQ FAQIQALYSM MATSLPAIIY SWGRNFMWSM
GIIRIGFMQD VFTWYVKSTG GTPSTLVDLG IHANVALAKR GIDLGSLAKR ATTTVTTSTS
DSITLRGIKR ISYMMGIETT NFFATGFSFF IILLFFSLLV AMASRFIVEM VLLASRNQAL
KKQRIRLYWK SISKGFFYRV IFVGFTQMSV LSMWEIYTRD SSALAFLSMY VIVDMAVLLC
YAFVRTIQII RKTGPYSHPD VLYNLYSDTQ HLMRWGFMYV QLDVRFFYFT FPLLLITLVR
SMFIGFGQGS PKVQGCAMFG ISVVVFALMV ILRPYATKHM NTLHIGVALM NLISGSFILV
MCQAFYVEEL ARQVIGIIFF ALNAITMLLL ILGIFIRTLI VLFRKSGHGT YYRILDDQSE
KATSYNKSIK DMSSSDMAFS DPAYSGTTLR SSVDLNTPEY PFSNRNDSDS TFTNNKYVSP
WDAIEEASYA NLRGNTDVEQ PFMESDYTRI SENNNNAERR RKPLPNNAFR
