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CHS2_SCHPO
ID   CHS2_SCHPO              Reviewed;         926 AA.
AC   O74756; Q9US88;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 141.
DE   RecName: Full=Chitin synthase-like protein 2;
GN   Name=chs2; ORFNames=SPBC1709.01, SPBC1734.17;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 720-925, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12914947; DOI=10.1016/s0014-5793(03)00812-3;
RA   Martin-Garcia R., Duran A., Valdivieso M.H.;
RT   "In Schizosaccharomyces pombe chs2p has no chitin synthase activity but is
RT   related to septum formation.";
RL   FEBS Lett. 549:176-180(2003).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15449309; DOI=10.1002/yea.1145;
RA   Matsuo Y., Matsuura Y., Tanaka K., Matsuda H., Kawamukai M.;
RT   "Chr4, a Schizosaccharomyces pombe homologue of the Saccharomyces
RT   cerevisiae Chs4p/Skt5p protein, is related to septum formation and is
RT   required for the proper localization of Chs2.";
RL   Yeast 21:1005-1019(2004).
CC   -!- FUNCTION: Plays a role in septum formation. Has no chitin synthase
CC       activity. {ECO:0000269|PubMed:12914947}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10759889,
CC       ECO:0000269|PubMed:12914947, ECO:0000269|PubMed:15449309}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:10759889,
CC       ECO:0000269|PubMed:12914947, ECO:0000269|PubMed:15449309}. Note=Septum.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA21311.1; -; Genomic_DNA.
DR   EMBL; AB027967; BAA87271.1; -; Genomic_DNA.
DR   PIR; T39629; T39629.
DR   PIR; T39664; T39664.
DR   RefSeq; NP_595434.1; NM_001021342.2.
DR   AlphaFoldDB; O74756; -.
DR   BioGRID; 276709; 21.
DR   STRING; 4896.SPBC1709.01.1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PaxDb; O74756; -.
DR   EnsemblFungi; SPBC1709.01.1; SPBC1709.01.1:pep; SPBC1709.01.
DR   GeneID; 2540176; -.
DR   KEGG; spo:SPBC1709.01; -.
DR   PomBase; SPBC1709.01; chs2.
DR   VEuPathDB; FungiDB:SPBC1709.01; -.
DR   eggNOG; KOG2571; Eukaryota.
DR   HOGENOM; CLU_004760_3_1_1; -.
DR   InParanoid; O74756; -.
DR   OMA; MYEFTST; -.
DR   PhylomeDB; O74756; -.
DR   PRO; PR:O74756; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR   GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR   GO; GO:0000935; C:division septum; IDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004100; F:chitin synthase activity; IGI:PomBase.
DR   GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0140278; P:mitotic division septum assembly; IC:PomBase.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR004834; Chitin_synth_fun.
DR   InterPro; IPR013616; Chitin_synth_N.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF01644; Chitin_synth_1; 1.
DR   Pfam; PF08407; Chitin_synth_1N; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell wall biogenesis/degradation; Membrane;
KW   Reference proteome; Septation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..926
FT                   /note="Chitin synthase-like protein 2"
FT                   /id="PRO_0000193717"
FT   TRANSMEM        564..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        599..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        641..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        671..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        721..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        853..873
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        885..905
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        734..737
FT                   /note="CMDP -> VWIL (in Ref. 2; BAA87271)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   926 AA;  105579 MW;  7B880751AD53115E CRC64;
     MSFQNPSYIN AKHRSFLQPK DTQDSQDLRN WVSHSSVDEE TAYSSSTLSS SSSKSFPCYD
     EYDEIKSPDD QKVEYMKTLR TLEEDAFSYT DSVYDFEERS FDEHEPPIPP LHKTGVFSVP
     LQPTHTVNSN SDDGYENSSK NEYLDFNSEI SASPVNEPMT HSQSYTSIDR LNSSSSHYSK
     DVPLLCGSLT IDCPTPIDLR GMLGPFMQKN PDEASFLRYS AITCQPEDMN NNGLQLRTWS
     TGRDIQIAVC LTLSDEDLAS FAISLSSIMN NLKHLCSRSK SRVWGNESWE KVLVCVVIDG
     RNTVHQNVLD LLASIGVYQP HIAKGRVNGK RTLSHMYEFT STINVDEKLN LTTATGDGNV
     PMQMLLCVKD RRLGTYNSHR WFLNGIASLA RPKVCLFVRN GARLGPTSIY HAWKAFDVDS
     TIGGMCGKTS IDTGKFGFRL LNPFIASQHF DQMIHNNLRL PYDSCMGYIS NALNAIYGFR
     YVALQDSYPN PGPLADYFEQ DQYEIPRRGI LQSNAFLAQE QLLFWKVITR KDAKWHLQYV
     PEACATIEAP NSMAGILESK KSEINSSFSL AVYVIVDFFS LWTTRHKFFR FLLLTVQSLV
     FAIEKLVNFF SMANFFLAFY FVCNATSYSS LNPYGNWARP LFLVFEYILI CLIFSQFMLA
     MGNRPRSCRV LLFISTALFS IIMIYFVFCV FYISLIPLHN SDNSEIVLGN NYFTTLIFSS
     LLILACYAFV SLICMDPFFI FTCIVQYILL MPTRIYTEQI YALCHLDDAS ISKDDNQQEF
     NFDTGITHCS MNDEGYTTIS IPKANVLNSV YNSSLKNFSS SNDTSVYHDV QDHCYRKPQS
     YEDHYQDIRT RYVLVWAVSN LILAIVLIQV FDGMRFINNG YMKYIFWSIV AFTAWKTMGA
     VTFIATKIIS RIANCVKSKL YIFNDP
 
 
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