CHS1_SCHPO
ID CHS1_SCHPO Reviewed; 859 AA.
AC P30597;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Chitin synthase 1;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
GN Name=chs1; ORFNames=SPAC13G6.12c, SPAC24B11.01c;
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 [GENOMIC DNA] OF 201-389.
RX PubMed=1731323; DOI=10.1073/pnas.89.2.519;
RA Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J.,
RA Robbins P.W.;
RT "Classification of fungal chitin synthases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA91105.1; -; Genomic_DNA.
DR EMBL; M82957; AAA35297.1; -; Genomic_DNA.
DR PIR; S62441; S62441.
DR RefSeq; NP_592838.1; NM_001018239.2.
DR AlphaFoldDB; P30597; -.
DR BioGRID; 279304; 3.
DR STRING; 4896.SPAC13G6.12c.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR MaxQB; P30597; -.
DR PaxDb; P30597; -.
DR EnsemblFungi; SPAC13G6.12c.1; SPAC13G6.12c.1:pep; SPAC13G6.12c.
DR GeneID; 2542858; -.
DR KEGG; spo:SPAC13G6.12c; -.
DR PomBase; SPAC13G6.12c; chs1.
DR VEuPathDB; FungiDB:SPAC13G6.12c; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_004760_3_1_1; -.
DR InParanoid; P30597; -.
DR OMA; AWILHYV; -.
DR PhylomeDB; P30597; -.
DR PRO; PR:P30597; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:PomBase.
DR GO; GO:0004100; F:chitin synthase activity; IMP:PomBase.
DR GO; GO:0034217; P:ascospore wall chitin biosynthetic process; IMP: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 InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF01644; Chitin_synth_1; 1.
DR Pfam; PF08407; Chitin_synth_1N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..859
FT /note="Chitin synthase 1"
FT /id="PRO_0000193716"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 273
FT /note="K -> R (in Ref. 2; AAA35297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 97990 MW; 63443713A7ADE421 CRC64;
MRRWFKKTLP RPPDEEESAG LTNKDIVETN HLYPTITNLS LNSDTSSILF DKNKKPLKPK
IIIPDKEFDL DYYLKDETES IQSPFEGFTA QPNFSNFNKQ GNTMNREANF QRTNEKIQRN
KSIKRVKLFH GNLILDCPIP KKLLVTLPQQ TEREFAYMRY SAATCDPQDF SKSLFTLRQP
LFFQPRKTEI CIAITMYNED EVLFARTMHS VMKNISHLCT RKNSQVWGKD AWKKVVVCII
SDGRTKIHPR TLAYLAAIGV YQDGIAKNQV NDKEVKAHIY EYTTQLSIDP NLKFKGSDRG
IVPVQMIFCL KEKNQKKLNS HLWFFQAFCP ILKPEVCILL DAGTRPGDQS IYHLWKSFDL
NPQVAGACGE IVVMKGKLGS GLINPLVATQ NFEYKMSNIL DKPVESVFGF ISVLPGAFSA
YRFEALQNDS QGNGPLASYF KGELQNTGKS GIFEANMYLA EDRILCFELV SKKNEAWILH
YVKSAYADTD VPDRIPEFVL QRRRWLNGSF FAAAYAICHY YRFFRTSHTI SRKFMLSIEF
IYQLATIVFG WFNIGNFFII FYILTSSLAS TSANFLPGEI LFRIAIWIYA SLLVTCFVLA
LGNRPHGSPN FYLSMVIMYS ILMGYLLFCS GWIAYRAISD AIHNASSTSS SYTSALLNSN
VFINIVISLS STYGMYLVVS IISFDPWHMF TSFVQYIFLS IMYTNVLNVY AFCNTHDVSW
GTKGDHFTNN DLGVARLLQK GADVEIAIPT NQSDIDAKYE DAVKLLASPS LEFNSPIINH
GEQEDFYKNF RTYVVLTWIL SNLFLVGIVL SIPKINGISI SNNETSAYLS FLLWSVVAFS
VFRFIGCIFY LFIRLCTGE
