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UniProtKB - Q01285 (CHS4_NEUCR)
Protein
Chitin synthase 4
Gene
chs-4
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Functioni
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
CuratedCatalytic activityi
- [(1→4)-N-acetyl-β-D-glucosaminyl](n) + UDP-N-acetyl-α-D-glucosamine = [(1→4)-N-acetyl-β-D-glucosaminyl](n+1) + H+ + UDPEC:2.4.1.16
GO - Molecular functioni
- chitin synthase activity Source: GO_Central
GO - Biological processi
- ascospore wall assembly Source: EnsemblFungi
- fungal-type cell wall chitin biosynthetic process Source: EnsemblFungi
- protein localization to bud neck Source: EnsemblFungi
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | Cell wall biogenesis/degradation |
Enzyme and pathway databases
BRENDAi | 2.4.1.16, 26170 |
Protein family/group databases
CAZyi | GT2, Glycosyltransferase Family 2 |
Names & Taxonomyi
Protein namesi | Recommended name: Chitin synthase 4 (EC:2.4.1.16)Alternative name(s): Chitin-UDP acetyl-glucosaminyl transferase 4 Class-IV chitin synthase 4 |
Gene namesi | Name:chs-4 ORF Names:NCU09324 |
Organismi | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Taxonomic identifieri | 367110 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:NCU09324 |
Subcellular locationi
Plasma membrane
- Cell membrane Curated; Multi-pass membrane protein Sequence analysis
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- cell periphery Source: GO_Central
- cell septum Source: GO_Central
- cellular bud neck Source: EnsemblFungi
- chitosome Source: EnsemblFungi
- incipient cellular bud site Source: EnsemblFungi
- integral component of membrane Source: UniProtKB-KW
- prospore membrane Source: EnsemblFungi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 212 | CytoplasmicCuratedAdd BLAST | 212 | |
Transmembranei | 213 – 233 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 234 – 244 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 245 – 265 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 266 – 514 | CytoplasmicCuratedAdd BLAST | 249 | |
Transmembranei | 515 – 535 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 536 – 1065 | ExtracellularCuratedAdd BLAST | 530 | |
Transmembranei | 1066 – 1086 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1087 – 1092 | CytoplasmicCurated | 6 | |
Transmembranei | 1093 – 1113 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1114 – 1116 | ExtracellularCurated | 3 | |
Transmembranei | 1117 – 1137 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1138 – 1235 | CytoplasmicCuratedAdd BLAST | 98 |
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000193704 | 1 – 1235 | Chitin synthase 4Add BLAST | 1235 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 639 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 1034 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 |
Keywords - PTMi
GlycoproteinProteomic databases
PRIDEi | Q01285 |
Structurei
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 203 | DisorderedSequence analysisAdd BLAST | 203 | |
Regioni | 545 – 592 | DisorderedSequence analysisAdd BLAST | 48 | |
Regioni | 645 – 670 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 1201 – 1235 | DisorderedSequence analysisAdd BLAST | 35 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 47 – 64 | Polar residuesSequence analysisAdd BLAST | 18 | |
Compositional biasi | 69 – 83 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 91 – 111 | Basic and acidic residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 143 – 200 | Basic and acidic residuesSequence analysisAdd BLAST | 58 | |
Compositional biasi | 548 – 565 | Basic and acidic residuesSequence analysisAdd BLAST | 18 | |
Compositional biasi | 1201 – 1219 | Polar residuesSequence analysisAdd BLAST | 19 |
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
HOGENOMi | CLU_002572_1_0_1 |
InParanoidi | Q01285 |
OMAi | FPLAHTM |
Family and domain databases
Gene3Di | 3.90.550.10, 1 hit |
InterProi | View protein in InterPro IPR004835, Chitin_synth IPR029044, Nucleotide-diphossugar_trans |
PANTHERi | PTHR22914, PTHR22914, 1 hit |
SUPFAMi | SSF53448, SSF53448, 1 hit |
i Sequence
Sequence statusi: Complete.
Q01285-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSLPRRPGPS PPHEEPRRYR QSGSRRSRPP PADVETGYAP MAGERPSQQQ
60 70 80 90 100
RVPSISSFPE TLPSPNPNVE RDPLAPTPEP AHPSGIPQRK RSLIRPERNR
110 120 130 140 150
IGKDHPNYHY RKHAANMNTL PSSTGHDPIY EDLEGATDDV SGTGSRNDDD
160 170 180 190 200
VSEESPPRRK HSTKMQVIET EKSGDERRRR RKSDTTKHGK IVKASKGKRE
210 220 230 240 250
KSGGLPTPSF WNIYCGFVTF WCPGFVLKCF GMPEMAQQRA WREKMGLISI
260 270 280 290 300
ILLIMGFVGF ITFGFTQVVC GKPPLRLRIN EVGSGYMIFH GSAYDLTKSH
310 320 330 340 350
HPPAEGIPRR PDGLGANVIY DLPQHYGGQD GSFLFQNVNG KCKGLITKQE
360 370 380 390 400
NSDVPSDKSG NLAWYFPCNT FNQDGSSKPN TTIPYYLGYA CHTTANARDS
410 420 430 440 450
FYLGLKSSAD VYFTWDDIKN SSRNLVVYSG HVLDLDLLHW FNDTQVTYPA
460 470 480 490 500
RFKELRDKNT AGNQAIRGRD ITHAFQSSKD KQIAECFEEI IKVGSVDTET
510 520 530 540 550
VGCIASKVVL YVSLVLILAV VLARFVLALI FQWFISKTYA AAKTSQTSDQ
560 570 580 590 600
RKRNRQIEDW TEDIYRAPPR LPGEVGSSVA GSSDRQSKRS SAFLPTHSRF
610 620 630 640 650
STVYGNERGN RKPGLPTTMA SQNAAGQLLH PGTIYGQGNE SRSSFLKSDA
660 670 680 690 700
YGSSSSPADG PGPAGFIHEA VVPQPPSDWM PFGFPLAHTI CLVTAYSEGE
710 720 730 740 750
MGVRTTLDSI AMTDYPNSHK VILVICDGII KGHGEEHSTP DIILGMMKDH
760 770 780 790 800
TIHPDDVEPF SYVAVATGSK RHNMAKVYTG FYDYGTNSAI PLEKQQRVPM
810 820 830 840 850
MMVVKCGTPA EASKSKPGNR GKRDSQIILM SFLQKVMFDE RMTELEYEMF
860 870 880 890 900
NGLWKITGIS PDFYEIVLMV DADTKVFPDS LTHMISAMVK DPEIMGLCGE
910 920 930 940 950
TKIANKRASW VSAIQVFEYF VSHHLAKAFE SVFGGVTCLP GCFCMYRIKA
960 970 980 990 1000
PKGAQNYWVP ILANPDVVEH YSENVVDTLH KKNLLLLGED RYLSTLMLRT
1010 1020 1030 1040 1050
FPKRKQVFVP QAVCKTTVPD EFMVLLSQRR RWINSTIHNL MELVLVRDLC
1060 1070 1080 1090 1100
GTFCFSMQFI VGIELIGTLV LPAAIAFTFY VVIISIINSP PQIIPLVLLG
1110 1120 1130 1140 1150
LILGLPAILV VVTAHSWSYI IWMFIYLLSL PVWNFVLPTY AFWKFDDFSW
1160 1170 1180 1190 1200
GDTRKTAGEK SSKGGHGEAE GEFDSSMITM KRWAEFERDR RVRSTYWAGS
1210 1220 1230
RDNVISGVGG SNGWGSSQPR GHEQGRHFDD YFSDA
Sequence cautioni
The sequence AAB03563 differs from that shown. Reason: Erroneous initiation.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 480 | D → Y in AAB03563 (PubMed:8628221).Curated | 1 | |
Sequence conflicti | 563 | D → E in AAB03563 (PubMed:8628221).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U25097 Genomic DNA Translation: AAB03563.1 Different initiation. CM002236 Genomic DNA Translation: ESA44002.1 CM002236 Genomic DNA Translation: ESA44003.1 |
PIRi | S61886 |
RefSeqi | XP_011393274.1, XM_011394972.1 XP_011393275.1, XM_011394973.1 |
Genome annotation databases
EnsemblFungii | ESA44002; ESA44002; NCU09324 ESA44003; ESA44003; NCU09324 |
GeneIDi | 3880177 |
KEGGi | ncr:NCU09324 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U25097 Genomic DNA Translation: AAB03563.1 Different initiation. CM002236 Genomic DNA Translation: ESA44002.1 CM002236 Genomic DNA Translation: ESA44003.1 |
PIRi | S61886 |
RefSeqi | XP_011393274.1, XM_011394972.1 XP_011393275.1, XM_011394973.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 5141.EFNCRP00000009136 |
Protein family/group databases
CAZyi | GT2, Glycosyltransferase Family 2 |
Proteomic databases
PRIDEi | Q01285 |
Genome annotation databases
EnsemblFungii | ESA44002; ESA44002; NCU09324 ESA44003; ESA44003; NCU09324 |
GeneIDi | 3880177 |
KEGGi | ncr:NCU09324 |
Organism-specific databases
VEuPathDBi | FungiDB:NCU09324 |
Phylogenomic databases
HOGENOMi | CLU_002572_1_0_1 |
InParanoidi | Q01285 |
OMAi | FPLAHTM |
Enzyme and pathway databases
BRENDAi | 2.4.1.16, 26170 |
Family and domain databases
Gene3Di | 3.90.550.10, 1 hit |
InterProi | View protein in InterPro IPR004835, Chitin_synth IPR029044, Nucleotide-diphossugar_trans |
PANTHERi | PTHR22914, PTHR22914, 1 hit |
SUPFAMi | SSF53448, SSF53448, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CHS4_NEUCR | |
Accessioni | Q01285Primary (citable) accession number: Q01285 Secondary accession number(s): Q7RVJ8, V5IPD9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | December 4, 2007 | |
Last modified: | February 23, 2022 | |
This is version 138 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families