CHS2_NEUCR
ID CHS2_NEUCR Reviewed; 1097 AA.
AC P30589; Q7RVF4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 4.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Chitin synthase 2;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 2;
GN Name=chs-2; ORFNames=NCU05239;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-1097.
RX PubMed=7952169; DOI=10.1099/13500872-140-9-2189;
RA Din A.B., Yarden O.;
RT "The Neurospora crassa chs-2 gene encodes a non-essential chitin
RT synthase.";
RL Microbiology 140:2189-2197(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 403-591.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA54816.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CM002239; EAA32767.3; -; Genomic_DNA.
DR EMBL; X77782; CAA54816.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M82951; AAA33582.1; -; Genomic_DNA.
DR PIR; B45189; B45189.
DR PIR; T47246; T47246.
DR RefSeq; XP_962003.3; XM_956910.3.
DR AlphaFoldDB; P30589; -.
DR STRING; 367110.P30589; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; EAA32767; EAA32767; NCU05239.
DR GeneID; 3878151; -.
DR KEGG; ncr:NCU05239; -.
DR VEuPathDB; FungiDB:NCU05239; -.
DR HOGENOM; CLU_004760_1_0_1; -.
DR InParanoid; P30589; -.
DR BRENDA; 2.4.1.16; 3627.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IBA:GO_Central.
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:1902406; P:mitotic actomyosin contractile ring maintenance; IEA:EnsemblFungi.
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 membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1097
FT /note="Chitin synthase 2"
FT /id="PRO_0000193702"
FT TOPO_DOM 1..748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..865
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..894
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..993
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 994..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1015..1025
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1026..1046
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1047..1097
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 495
FT /note="K -> M (in Ref. 2; CAA54816 and 3; AAA33582)"
FT /evidence="ECO:0000305"
FT CONFLICT 939
FT /note="G -> V (in Ref. 2; CAA54816)"
FT /evidence="ECO:0000305"
FT CONFLICT 974..977
FT /note="AVPV -> CRSL (in Ref. 2; CAA54816)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="R -> K (in Ref. 2; CAA54816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1097 AA; 123135 MW; 8EF4FC97A6663EE8 CRC64;
MAGYGHSTAG GFGSGSGSGP PGPQYMLPQY DEGDDPDADA TPAGQGVRLL TNLDNSSYIS
VSEITSQSSH RDNIRPSRLR QAYEPSIDAR TYEPSLDTRT YEPSISDRRH MYEPSIDERS
SYMDPPRIPP PDGGSYVSSY MGTESMVSGH GRPWSPESAT GYRVPPQGRY EPSEIDGHAR
PGTPGSSYGN ARRPLPSAPA PLHYNSPSRA ASHYPRYHGG YADDVTVSMG PDDDRTDIFG
PETDLSETRH LNDAYGFRSS QITLSEDPHG THARSRYDDE DDVSTTYSSN TGTSASGVDK
FEHYGPIPEE GKHERRGVRP PQMSRKEVQL INGELVLECK IPTILYSFLP RRDEVEFTHM
RYTAVTCDPD DFVARGYKLR QNIGRTARET ELFICVTMYN EDEFGFTRTM HAVMKNISHF
CSRNKSRTWG ADGWQKIVVC VVSDGREIIH PRTLDALAAM GVYQHGIAKN FVNQKAVQAH
VYEYTTQVSL DSDLKFKGAE KGIVPCQMIF CLKEKNQKKL NSHRWFFNAF GKALNPNVCI
LLDVGTRPGG TSLYHLWKAF DTDSNVAGAC GEIKAMKGRF GGNLLNPLVA SQNFEYKMSN
ILDKPLESVF GYITVLPGAL SAYRYHALQN DETGHGPLSQ YFKGETLHGQ HADVFTANMY
LAEDRILCWE LVAKRGERWV LKYVKGCTGE TDVPDTVPEF VSQRRRWLNG AFFAAVYSLV
HFRQIWKTDH TFMRKALLHV EFLYHLLQLL FTYFSLANFY LAFYFIAGGL ADPHVDPFNS
DGHVARIIFN ILRYVCVLLI CTQFILSLGN RPQGAKRMYL ASMIIYAVIM VYTTFATIFI
VVRQIQPSQK SDDKPDLELG NNVFTNLIVS VASTLGLYFV MSFLYLDPWH MFTSAIQYFV
LLPSYICTLQ IYAFCNTHDV TWGTKGDNVM RTDLGGAIGK GSTVELEMPS DQLDIDSGYD
ECLRNLRDRV MVPAVPVSED QLQQDYYKSV RTYMVVSWMV ANATLAMAVS EAYGDSEIGD
NFYLRFILWA VAALALFRAL GSTTFAAINL VSALVEGRVR LRLNMKGFRW IKEKWGDADV
KGKFEGLGDR ARGLARR
