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Protein

Cell wall alpha-1,3-glucan synthase mok12

Gene

mok12

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

UDP-glucose + (alpha-D-glucosyl-(1->3))(n) = UDP + (alpha-D-glucosyl-(1->3))(n+1).

GO - Molecular functioni

  • alpha-1,3-glucan synthase activity Source: PomBase
  • alpha-amylase activity Source: PomBase

GO - Biological processi

  • (1->3)-alpha-glucan biosynthetic process Source: PomBase
  • alpha-glucan biosynthetic process Source: PomBase
  • ascospore wall assembly Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.
GT5. Glycosyltransferase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell wall alpha-1,3-glucan synthase mok12 (EC:2.4.1.183)
Gene namesi
Name:mok12
ORF Names:pi011, SPBC32H8.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC32H8.13c.
PomBaseiSPBC32H8.13c. mok12.

Subcellular locationi

GO - Cellular componenti

  • ascospore wall Source: PomBase
  • Golgi apparatus Source: PomBase
  • prospore membrane Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23522352Cell wall alpha-1,3-glucan synthase mok12PRO_0000080330Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi276775. 2 interactions.
MINTiMINT-4715149.

Structurei

3D structure databases

ProteinModelPortaliQ9UUL4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase group 1 family.Curated

Phylogenomic databases

HOGENOMiHOG000163916.
KOiK00749.
OrthoDBiEOG7BZW1K.
PhylomeDBiQ9UUL4.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001296. Glyco_trans_1.
IPR017853. Glycoside_hydrolase_SF.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF00128. Alpha-amylase. 1 hit.
PF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9UUL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFFSIPTIL LIFFLFIQII TAAFLTDENE PWNLNRNWTA QKILDYSAEW
60 70 80 90 100
NSHEYFPSPS NWRALPFYTI ILDKWTNGVP ENDVAEDTVF ESDPYEVTFR
110 120 130 140 150
AGGDIVGLVT PRSLDYLESM GIKAVYIAGT PFQNLPWYPD GYSPLDFTLL
160 170 180 190 200
DKHTGTLNQW HEAIMKLHER GFYVVVDFTI STLSELSYFV NSSMSFANTS
210 220 230 240 250
APFSTKGYKM KYKHPEYHYT DFQLSNGSSY SCNAPTFWDV TGLPINNTED
260 270 280 290 300
LNSISEVMCL SGDFDHYGDV EAFGNHPPWW RQLSNFASVQ DRLRDWDPIV
310 320 330 340 350
AKKLKHLGCL AVKMLDIDGI RVDKATQITA DFLGDWSAYI RQCAREIGKE
360 370 380 390 400
NFFIPGEVTS GADFGSIYVG RGRQADQRPN NREIALQTGY NESKYFLRKE
410 420 430 440 450
SDSALDSVSF HYSVYRTLTL LLGLQGELFA AFDLNRHDFA AMWNQMLIQD
460 470 480 490 500
DMINANTKKF DPRHLYGLTN QDIFRWPSIK DGRFKQLLGL FVVHLLMPGI
510 520 530 540 550
PLIYYGEEQN LKLLDNQAAN YIFGRQPITS SIGWQKHGCY QIGTTQYTDL
560 570 580 590 600
DFGPASEACR DDWNSLDHLD PTSPTKHYIA RMNEIRSYFP QVRDGWDLKL
610 620 630 640 650
IGKWTHEGTF PGNELYGESN PTTWGLWSMI RGPLAPYQKF SDQNDYIWLI
660 670 680 690 700
FTNENTTKTY DMDCMRQVDN KFPPYPALLG PYSSGSTVKN LLYPYEEIDL
710 720 730 740 750
STSTIDSPDI GNIGCIPHLT IDAYGSKIFV KKEDWIRPSL YLTKFLPGHD
760 770 780 790 800
SRIYSATEVT SFKISLGFSE EVDCKDLFKR IGFNSRTLNS SFAPKILEDS
810 820 830 840 850
ISCGYLDQPA PQEYTNAPVT KWFFNATLDS VPNGMHELLL NEVKSTSNQT
860 870 880 890 900
MQSKIARLIF RVGNEENPLV YPNNATFSPS LLYKASNGDL YVNHTGAGAD
910 920 930 940 950
KYRFSLNYGG TYSKWKTVST PSEKLRKPTW NGTNLQKWDG DHLIVQYWSS
960 970 980 990 1000
IALSTAHVQH GDTLNYSRQF PNLFVQGAFN RFGYDGSMPS KMSYNLENRT
1010 1020 1030 1040 1050
WSYDLISTWP AELVLNVWGM NPDNNADQGW VYGDLDNDTI IDRVPPGSSR
1060 1070 1080 1090 1100
ISNFIRFLDP PPKPYLSYKM YLNDFTRQLH YIPKGSWTVQ IVAIVLLILL
1110 1120 1130 1140 1150
PPLFGIFSVA LYSGAFSRVT IFNGSHNRGI KVAKQKIKSI MSRIFPFSVH
1160 1170 1180 1190 1200
LPLDNSSELL KQLPESEKRL NVLVATLEYD VPDLGIRVKI GGLGVMAQLM
1210 1220 1230 1240 1250
GQHMEFQDMV WVVPIISGVE YPFDKLCTEP KIAVKIGDDE FVVNCYSYKS
1260 1270 1280 1290 1300
GNITYVFLQS EVFYKQSSKE PYPLKMDDLA SAIFYSVWNQ CIAEVWKRFP
1310 1320 1330 1340 1350
LDIYHVNDYH GALAPLYLLP EVIPVAVSLH NAEFQGLWPL RTSAELECVC
1360 1370 1380 1390 1400
SIFNIEKDIC TKYVQFGHVF NLLHSIISYV RKHQGGYGVV AVSDKYSKQT
1410 1420 1430 1440 1450
LSRYPIFWSL VHISGLPNPD PSDLKLLNHL TDDPVDVDFV LEAKRKLLKK
1460 1470 1480 1490 1500
QTQEWANLDV DPSAQLLVFV GRWSHQKGID LIADLAPKLL TEHNVQLITI
1510 1520 1530 1540 1550
GPVIDLHGQF AAEKLEQIAK RFPTRVLCKP VFTAVPPFLF AGTDFALIPS
1560 1570 1580 1590 1600
RDEPFGLVAV EFGRKGVLCI GSRTGGLGHM PGWWFQMASP NTGHLLTQFE
1610 1620 1630 1640 1650
NAITKALHSN GELRARLRVE ALRQRFPVCI WKQKSENLLK SCIYVHEMET
1660 1670 1680 1690 1700
LKHASPTFKA YQFVVRICHY LTSKVKSINK DQVFNAFSPD VSERPPLFEV
1710 1720 1730 1740 1750
ASCSNETDSV EKLTPELSVS PESDMHFKDG NSSKLEIVES KEIYASDSDI
1760 1770 1780 1790 1800
SNSTSEDINK DECVSKDIEV DNFALNLQSQ SYEGDSNDFG IREVPLSDAN
1810 1820 1830 1840 1850
QSSQADSTSI DRYGPYSSQK VNFSKYKDFV ESRPTFFQSS VTFTDADGST
1860 1870 1880 1890 1900
RKTFSKRLEN LTTSNTLKSL SVDHFIRKHE RKYFNGLRKQ EIDVKLKSRS
1910 1920 1930 1940 1950
DKEKSCTVSE SYKQIDCDTY EATRLQKLLL HSIGGWPLYT IVLAIGQILG
1960 1970 1980 1990 2000
ASSYQLTLLS GESAQSTVSM YILLSIFSFF SLFWWFLSRV VQARYILSLP
2010 2020 2030 2040 2050
FFFFGISFIL VAITHFFQKT TACSVIQHIA AYVYAISSST GSLYFAWNFG
2060 2070 2080 2090 2100
AEGGIATHHW ILRACLVHGI QQIWSAILWS WGDLLSKKDL TQNVGPGIFA
2110 2120 2130 2140 2150
GGLIASFICF GLSYVTFAGL PAFYRQAPSI IPAFYRSLGK RNIVIWFFIS
2160 2170 2180 2190 2200
QILINYWLAV PYGQAWRFFW NTSNTPLWSI IILLLIFFIV VWAVLLSVIK
2210 2220 2230 2240 2250
ILSLNNVWFP VIFGLGLICP RWCLEFWSSS GLGINLPWAG KASALLTKSV
2260 2270 2280 2290 2300
WLLLALWDGI QGVGVGVMLL QTLARDHVAF TLMLAQVISC ITIMIAKPSL
2310 2320 2330 2340 2350
PVSDRVFPNL GAWNPSEGPG PCASPCFYIA LICQFVAVGG LLYHYRKSQL

AL
Length:2,352
Mass (Da):266,564
Last modified:May 1, 2000 - v1
Checksum:i78ADF9C2F7140BBA
GO

Sequence cautioni

The sequence BAA21388.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018381 Genomic DNA. Translation: BAA76558.1.
AB004534 Genomic DNA. Translation: BAA21388.1. Different initiation.
CU329671 Genomic DNA. Translation: CAC37503.1.
PIRiT43431.
RefSeqiNP_595619.1. NM_001021514.2.

Genome annotation databases

EnsemblFungiiSPBC32H8.13c.1; SPBC32H8.13c.1:pep; SPBC32H8.13c.
GeneIDi2540243.
KEGGispo:SPBC32H8.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018381 Genomic DNA. Translation: BAA76558.1.
AB004534 Genomic DNA. Translation: BAA21388.1. Different initiation.
CU329671 Genomic DNA. Translation: CAC37503.1.
PIRiT43431.
RefSeqiNP_595619.1. NM_001021514.2.

3D structure databases

ProteinModelPortaliQ9UUL4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276775. 2 interactions.
MINTiMINT-4715149.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.
GT5. Glycosyltransferase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC32H8.13c.1; SPBC32H8.13c.1:pep; SPBC32H8.13c.
GeneIDi2540243.
KEGGispo:SPBC32H8.13c.

Organism-specific databases

EuPathDBiFungiDB:SPBC32H8.13c.
PomBaseiSPBC32H8.13c. mok12.

Phylogenomic databases

HOGENOMiHOG000163916.
KOiK00749.
OrthoDBiEOG7BZW1K.
PhylomeDBiQ9UUL4.

Miscellaneous databases

PROiQ9UUL4.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001296. Glyco_trans_1.
IPR017853. Glycoside_hydrolase_SF.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF00128. Alpha-amylase. 1 hit.
PF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fission yeast alpha-glucan synthase Mok1 requires the actin cytoskeleton to localize the sites of growth and plays an essential role in cell morphogenesis downstream of protein kinase C function."
    Katayama S., Hirata D., Arellano M., Perez P., Toda T.
    J. Cell Biol. 144:1173-1186(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment."
    Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.
    Yeast 16:71-80(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiMOK12_SCHPO
AccessioniPrimary (citable) accession number: Q9UUL4
Secondary accession number(s): O13605
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.