MOR2_SCHPO
ID MOR2_SCHPO Reviewed; 2196 AA.
AC Q9HDV6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cell polarity protein mor2;
DE AltName: Full=Morphological round protein 2;
GN Name=mor2; ORFNames=SPBP19A11.04c;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=12234926; DOI=10.1093/emboj/cdf495;
RA Hirata D., Kishimoto N., Suda M., Sogabe Y., Nakagawa S., Yoshida Y.,
RA Sakai K., Mizunuma M., Miyakawa T., Ishiguro J., Toda T.;
RT "Fission yeast Mor2/Cps12, a protein similar to Drosophila Furry, is
RT essential for cell morphogenesis and its mutation induces Wee1-dependent G2
RT delay.";
RL EMBO J. 21:4863-4874(2002).
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).
CC -!- FUNCTION: Required for the maintenance of cell polarity. Has a role in
CC localizing F-actin at the cell tips. {ECO:0000269|PubMed:12234926}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12234926}. Membrane
CC {ECO:0000269|PubMed:12234926}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12234926}. Note=Found at the cell tips and at the
CC site of septum formation.
CC -!- SIMILARITY: To yeast TAO3/PAG1. {ECO:0000305}.
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DR EMBL; AB093007; BAC20935.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC19754.1; -; Genomic_DNA.
DR RefSeq; NP_596172.1; NM_001022092.2.
DR AlphaFoldDB; Q9HDV6; -.
DR SMR; Q9HDV6; -.
DR BioGRID; 277829; 12.
DR STRING; 4896.SPBP19A11.04c.1; -.
DR iPTMnet; Q9HDV6; -.
DR MaxQB; Q9HDV6; -.
DR PaxDb; Q9HDV6; -.
DR PRIDE; Q9HDV6; -.
DR EnsemblFungi; SPBP19A11.04c.1; SPBP19A11.04c.1:pep; SPBP19A11.04c.
DR GeneID; 2541317; -.
DR KEGG; spo:SPBP19A11.04c; -.
DR PomBase; SPBP19A11.04c; mor2.
DR VEuPathDB; FungiDB:SPBP19A11.04c; -.
DR eggNOG; KOG1825; Eukaryota.
DR HOGENOM; CLU_000325_1_0_1; -.
DR InParanoid; Q9HDV6; -.
DR OMA; HAQQVTI; -.
DR PhylomeDB; Q9HDV6; -.
DR PRO; PR:Q9HDV6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0062200; P:RAM/MOR signaling pathway; IMP:PomBase.
DR GO; GO:2000100; P:regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025614; Cell_morpho_N.
DR InterPro; IPR025481; Cell_Morphogen_C.
DR InterPro; IPR039867; Furry/Tao3/Mor2.
DR InterPro; IPR029473; MOR2-PAG1_mid.
DR PANTHER; PTHR12295; PTHR12295; 1.
DR Pfam; PF14225; MOR2-PAG1_C; 1.
DR Pfam; PF14228; MOR2-PAG1_mid; 3.
DR Pfam; PF14222; MOR2-PAG1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 4: Predicted;
KW Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..2196
FT /note="Cell polarity protein mor2"
FT /id="PRO_0000096536"
SQ SEQUENCE 2196 AA; 251198 MW; AAF2698DB00DE4CF CRC64;
MSLNEIAHDQ PVENGPLYSE KQDHTAVDYA LHILFTQFVR LSEQKISFLS RYHANEGKNA
EPVRFNVGEQ EAILLLKKGE DNEFDRCIQA LVALASSKPV AVIESLLCWR KVRVDITSSS
GTPRVVNERR SSISIYILCR VLTEIAETIP SNALEESTVS CLLECVFHQL LSAKNLPVSS
SYFSLANWES FAFLVGSMSR FNFVMVSDRF IEEIEHLEKS GCDSRQKETV LVHLLRAMRY
LRLQLYPTTL LEESIAFLQS LTSFFMKANT ALKIEYAYLM EQLLRPLISR ATFEVNIPAW
SRTIETIYPV VLKMCTKTKY WNVFFPFCCT LLCLSPKQFF LKHWISSLDA AFFRVKDRRL
RNTGLPHLSR VVWTYSNQYK EEPSIMNSNI SNILKSGFSI GKKFSVVPFA TLEELDGYAQ
IVRVVGAHFP ELVIKEILTP LSTDAFTENI GPEKLMIVVR SVYYILHDMK YKKSDSTIFE
YIEFEFVDLH EVAVGTPLQQ FVHNLSQKLL FLVFQLSTNT NCYLDSKNAT SLLALYINAL
KVFPCLMGKL EQRVIDAYVK CLNCSNKIIH TVCHNSLIYF SSGLKMSKSV ISCLSRKLVK
GSEYLLRTYH EVIRIWISQQ EAVIEKRNSV LSNKSCASSE SNTPASVKQD YDDIQSWTII
EEIQSLGVLH LSSPSVGIRK FAVALLNDVK QLNTEYLMLS SDKVEVGDIY SEPTIVDVLK
DCDSSILSVE SHLPTAAERS RLRKFINDGT KDMLLKLATS NSGVDISIWY NVFPRFIKVC
FERFPTTMAL LRNTVCEKLP SITMQLLSRI ESSELNFNLK SAVKNDNFPE FLLVQWKLYL
IVACCTITYT SNVDYSHTDL RRTLTAVQSG NHLRGLQETI KITSAESLFS MVLPLIFTEF
SPIREAVVFA IGCINVNAFP QLVRSLKPYI SVLKQDHQEF IFAGLNFPSV KRRNKPDLLL
RSEIAHIFAM TSHLLLHELL NEDREALSVI SEFLKDLKGF LSTPNVQADE KYLKLRCYFS
QLLEKVLLVQ NLHPSSEVLP FSGRASCWKL LDEWTGFGPA RAITKNREEL MRAHIRGNNK
DIRERDKLLA SFEAGKQNLE YLAIKAMIAL CTAKLQQELT EGVFLFDIEI LLNWFTAVFG
SPSKAIVGLA RKGLTALLLE NSSNEVLLQK VINRCFSKEI SQTISNYYFL SLSEMLIQIN
PNNLSKPKLL PLCLVNLSTN NLSVRLKAFE LLGNFHLNNF TMTALMEFKT FLESSNPALY
LKPQYLFSVQ LASDFTEDSF TLTSECLRYF NYGHQHRRGL VTVLLPWLQN LELKMDVENK
TFDSFTAVIL IDLIEVTAKF TNDLPNEIEA LWTSLALSRH KSNWTVILFF LMQQCYQRKT
FSFVDCTRQI TIYLAKTELL SDLYSTLLSF VCPANVSNEN QEVYKFSLED LSSTYVANLE
DLFPSEKNHI SYSPCQLSLL LLMDILPNPS IITVTDDVAT ILHAAFIQFD HYSRIVQEQC
QQIFQYVVRK VLAMEGRLDY DDAYFDFNVE SSLITGLRGK TKKEDDLVKY HNMILKTIEL
LSSSYPELKQ IWGEVALSWA TTCPSRRLAC NSFQLFRSLL PDFDARMLLE IISRLVGTIS
DETSYLRDYS VEILRTFNSY VLVMNSDDLL SYSQILWTAI ACLTTIHEDE FIESVKIAYA
YFLRVEETDS ATQQIMETFP QNWVGDYQGL QILILKGFRS TNSFEITMNF FLLLMDFKDN
DLVGVGYLRI LSCLLVSLPA MVYTYEHSDP ITFDLSVFCH KLATLASQFN DDALIELLDT
YLKRKFRSIK DFLKHTVSYL YSYYFEDYEL EIVSTLTMFL SNNLTWFRKS TLDVLKELFP
LIDFQKPIYS EHGLGIVSPL LRLLPTGYAM EALSLLTDSV LHVSAPTDMQ TLKLLMVDPK
LKNSDDRLAG FFEIPDEDGW YEPNSEYAAA ITKSNVHAVF YSCSTTEASV STPEVRFHAD
EVSNYPRHVP TDSHGSLDEN SLGELVTTLH SLDVFFAEDR DEELIQPDVA VDPKLDITSE
DYDDRIATIL SGSLRRQKQG LMAYETESFR DYSPNEEIDA SAKLPMDMPP VRVRKSSFIS
KLKPHYFMDA ESYYPSLKAL GNSAEHRLSL DEIRGAAELK QNKNWNSMLD QSVSMINEDS
VEDHETHENY YHLRTMFQGS ESNESFTDTT RSRGWH