CHS4_NEUCR
ID CHS4_NEUCR Reviewed; 1235 AA.
AC Q01285; Q7RVJ8; V5IPD9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chitin synthase 4;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 4;
DE AltName: Full=Class-IV chitin synthase 4;
GN Name=chs-4; ORFNames=NCU09324;
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 [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8628221; DOI=10.1007/bf02174181;
RA Din A.B., Specht C.A., Robbins P.W., Yarden O.;
RT "chs-4, a class IV chitin synthase gene from Neurospora crassa.";
RL Mol. Gen. Genet. 250:214-222(1996).
RN [2]
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).
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. Class IV subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03563.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U25097; AAB03563.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM002236; ESA44002.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA44003.1; -; Genomic_DNA.
DR PIR; S61886; S61886.
DR RefSeq; XP_011393274.1; XM_011394972.1.
DR RefSeq; XP_011393275.1; XM_011394973.1.
DR AlphaFoldDB; Q01285; -.
DR STRING; 5141.EFNCRP00000009136; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; Q01285; -.
DR EnsemblFungi; ESA44002; ESA44002; NCU09324.
DR EnsemblFungi; ESA44003; ESA44003; NCU09324.
DR GeneID; 3880177; -.
DR KEGG; ncr:NCU09324; -.
DR VEuPathDB; FungiDB:NCU09324; -.
DR HOGENOM; CLU_002572_1_0_1; -.
DR InParanoid; Q01285; -.
DR OMA; DIMGLCG; -.
DR BRENDA; 2.4.1.16; 3627.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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:0045009; C:chitosome; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; 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:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0004100; F:chitin synthase activity; IBA:GO_Central.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR SUPFAM; SSF53448; SSF53448; 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..1235
FT /note="Chitin synthase 4"
FT /id="PRO_0000193704"
FT TOPO_DOM 1..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..1065
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1066..1086
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1087..1092
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1114..1116
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1138..1235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 480
FT /note="D -> Y (in Ref. 1; AAB03563)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="D -> E (in Ref. 1; AAB03563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1235 AA; 137990 MW; F275C6603FB8CDD4 CRC64;
MSLPRRPGPS PPHEEPRRYR QSGSRRSRPP PADVETGYAP MAGERPSQQQ RVPSISSFPE
TLPSPNPNVE RDPLAPTPEP AHPSGIPQRK RSLIRPERNR IGKDHPNYHY RKHAANMNTL
PSSTGHDPIY EDLEGATDDV SGTGSRNDDD VSEESPPRRK HSTKMQVIET EKSGDERRRR
RKSDTTKHGK IVKASKGKRE KSGGLPTPSF WNIYCGFVTF WCPGFVLKCF GMPEMAQQRA
WREKMGLISI ILLIMGFVGF ITFGFTQVVC GKPPLRLRIN EVGSGYMIFH GSAYDLTKSH
HPPAEGIPRR PDGLGANVIY DLPQHYGGQD GSFLFQNVNG KCKGLITKQE NSDVPSDKSG
NLAWYFPCNT FNQDGSSKPN TTIPYYLGYA CHTTANARDS FYLGLKSSAD VYFTWDDIKN
SSRNLVVYSG HVLDLDLLHW FNDTQVTYPA RFKELRDKNT AGNQAIRGRD ITHAFQSSKD
KQIAECFEEI IKVGSVDTET VGCIASKVVL YVSLVLILAV VLARFVLALI FQWFISKTYA
AAKTSQTSDQ RKRNRQIEDW TEDIYRAPPR LPGEVGSSVA GSSDRQSKRS SAFLPTHSRF
STVYGNERGN RKPGLPTTMA SQNAAGQLLH PGTIYGQGNE SRSSFLKSDA YGSSSSPADG
PGPAGFIHEA VVPQPPSDWM PFGFPLAHTI CLVTAYSEGE MGVRTTLDSI AMTDYPNSHK
VILVICDGII KGHGEEHSTP DIILGMMKDH TIHPDDVEPF SYVAVATGSK RHNMAKVYTG
FYDYGTNSAI PLEKQQRVPM MMVVKCGTPA EASKSKPGNR GKRDSQIILM SFLQKVMFDE
RMTELEYEMF NGLWKITGIS PDFYEIVLMV DADTKVFPDS LTHMISAMVK DPEIMGLCGE
TKIANKRASW VSAIQVFEYF VSHHLAKAFE SVFGGVTCLP GCFCMYRIKA PKGAQNYWVP
ILANPDVVEH YSENVVDTLH KKNLLLLGED RYLSTLMLRT FPKRKQVFVP QAVCKTTVPD
EFMVLLSQRR RWINSTIHNL MELVLVRDLC GTFCFSMQFI VGIELIGTLV LPAAIAFTFY
VVIISIINSP PQIIPLVLLG LILGLPAILV VVTAHSWSYI IWMFIYLLSL PVWNFVLPTY
AFWKFDDFSW GDTRKTAGEK SSKGGHGEAE GEFDSSMITM KRWAEFERDR RVRSTYWAGS
RDNVISGVGG SNGWGSSQPR GHEQGRHFDD YFSDA
