RAX2_SCHPO
ID RAX2_SCHPO Reviewed; 1155 AA.
AC O14239;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Polarized growth protein rax2;
DE AltName: Full=Revert to axial protein 2;
DE Flags: Precursor;
GN Name=rax2; ORFNames=SPAC6F6.06c;
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 FOR3 AND TEA1, AND SUBCELLULAR LOCATION.
RX PubMed=17085965;
RA Choi E., Lee K., Song K.;
RT "Function of rax2p in the polarized growth of fission yeast.";
RL Mol. Cells 22:146-153(2006).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Controls cell polarity, through the G1 phase of mitosis, via
CC regulation of for3 localization. Required for actin cable formation
CC where it directs the spatial distribution of the actin cables.
CC {ECO:0000269|PubMed:17085965}.
CC -!- SUBUNIT: Interacts with for3 and tea1. {ECO:0000269|PubMed:17085965}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:17085965}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17085965}.
CC Note=Localizes at the cell cortex of the 'old' growing cell tips.
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DR EMBL; CU329670; CAB11730.1; -; Genomic_DNA.
DR PIR; T39040; T39040.
DR RefSeq; NP_593899.1; NM_001019329.2.
DR AlphaFoldDB; O14239; -.
DR BioGRID; 279241; 2.
DR STRING; 4896.SPAC6F6.06c.1; -.
DR SwissPalm; O14239; -.
DR MaxQB; O14239; -.
DR PaxDb; O14239; -.
DR EnsemblFungi; SPAC6F6.06c.1; SPAC6F6.06c.1:pep; SPAC6F6.06c.
DR GeneID; 2542793; -.
DR KEGG; spo:SPAC6F6.06c; -.
DR PomBase; SPAC6F6.06c; rax2.
DR VEuPathDB; FungiDB:SPAC6F6.06c; -.
DR eggNOG; ENOG502QQZD; Eukaryota.
DR HOGENOM; CLU_276484_0_0_1; -.
DR InParanoid; O14239; -.
DR OMA; NASMPYW; -.
DR PhylomeDB; O14239; -.
DR PRO; PR:O14239; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; NAS:PomBase.
DR GO; GO:1902929; C:plasma membrane of growing cell tip; IDA:PomBase.
DR GO; GO:0061572; P:actin filament bundle organization; IMP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0061161; P:positive regulation of establishment of bipolar cell polarity regulating cell shape; IMP:PomBase.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1155
FT /note="Polarized growth protein rax2"
FT /id="PRO_0000290655"
FT TOPO_DOM 28..1105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 876
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1055
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1155 AA; 128334 MW; 74E6980F1A452A5E CRC64;
MAIYSSFWIR LYFTFRFFCY FLTSVVASDV SFLGDFSGFN VLSNSSANTD LSSQFFEQTN
NGSLSSLIDT SYSNSQICYS SWQGDLYVIV LDSEQQTVLL QSNFTSNPTS LEIFSSQNTS
FFGNISAIFC DDKFPYAYAT FTFSDKPSFT SIYRWNVTNS NVTIEHFYNV KGNVDSLFFL
NNDSVAISGN FTEISPFSSS NGPQIAKLAF RSNNSFSQNS LNRNLSSVSC DLTDSYSLWD
PSSSGLVSIY AWAPYLIDFN RIRFYNYESS ENSVAFFSAI NPADGTVLPL THYDLETGLS
STCDVNCSLQ NFANYQDFYF SKGYNSYQIE IQMFGNGEAT ENSAFGLSSL QFFETNQNSY
FDDSYNQESC GFPGLNSLSS YEGNFEASFS NASMPYWIQT IAGEQASVSF FPNITVPTNG
TVQLLIPGCT YDNTCSQRGS VIANVYFAKN KQPATKLVQQ ASDFDQYVSL YSGYLQGFSD
NFRPYVELLP YKNSRMVTHS IRFLEQSYTN VSNGLVFVNT TTDVNKLPSI IEFPAASKLR
GTAISQIKSL SNGNFSLYMT GNFSDNYGNN VVYMDSLNHL HSFPNNGLNG WVSYIYVSGD
SSYFGGNFTH TGDGSIKLNY IAMYSETSRN WSSLGLGTNG PVTHIGSTSL FIDGKIESFI
SFQGDFNEVY TSEGYAISTS GFSLWNPSSK SWVSMEKLGF YMSGYLFDIP GFNSTQRIYS
GNLSAIASYS TRNIAHFSSD SLNDTFIPCY VNAFPSYIRL EDIAYPFANN SMIAILGSEE
MEDKCTAAVY FANSTEPIYP KRILSANCSS KFIVLEDCLI IYSNDTDESD IVKNTFVSFN
TTSNSLGNTT ALSQLKGHIN SVIVDDSYNN IFFGGNLSEQ SSGCVGFCIF EYNSSSWRNI
SHNLISAEVQ SILWVNETYS SMYLAGKFVW DTSDVDYLLM YNFDNNTIMS CKGSSSIPGP
VLLASLKSQS KDEYSVLLYG TEVSSSDTYL NVLNSEGAIN SYSLDIHLNQ STINSIDFFE
SNQISQIPIN DSIIVLSGLI VLDDSSKASA VYCVNKSCLP LLTAFKDNGE AGIVRKVVQQ
KSFSSSASKM IPVTTKYDHI GQPRYVVIIS LGISIGVMFL IMSGSIVVEI IHWFFSEHVE
TLHDYSNFLK ELKTQ
