ID CHS5_EXODE Reviewed; 1885 AA. AC Q8TGV2; DT 02-OCT-2024, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 27-NOV-2024, entry version 89. DE RecName: Full=Chitin synthase 5 {ECO:0000303|PubMed:14871935}; DE EC=2.4.1.16 {ECO:0000269|PubMed:18992354, ECO:0000269|PubMed:19431044}; DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 5 {ECO:0000305}; DE AltName: Full=Class-V chitin synthase 5 {ECO:0000303|PubMed:14871935}; GN Name=CHS5 {ECO:0000303|PubMed:14871935}; OS Exophiala dermatitidis (Black yeast) (Wangiella dermatitidis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala. OX NCBI_TaxID=5970; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND DISRUPTION RP PHENOTYPE. RC STRAIN=8656; RX PubMed=14871935; DOI=10.1128/ec.3.1.40-51.2004; RA Liu H., Kauffman S., Becker J.M., Szaniszlo P.J.; RT "Wangiella (Exophiala) dermatitidis WdChs5p, a class V chitin synthase, is RT essential for sustained cell growth at temperature of infection."; RL Eukaryot. Cell 3:40-51(2004). RN [2] RP INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12213927; DOI=10.1099/00221287-148-9-2811; RA Wang Q., Liu H., Szaniszlo P.J.; RT "Compensatory expression of five chitin synthase genes, a response to RT stress stimuli, in Wangiella (Exophiala) dermatitidis, a melanized fungal RT pathogen of humans."; RL Microbiology 148:2811-2817(2002). RN [3] RP INDUCTION. RX PubMed=17937668; DOI=10.1111/j.1574-6968.2007.00920.x; RA Liu H., Szaniszlo P.J.; RT "Transcription and expression analyses of WdCHS5, which encodes a class V RT chitin synthase with a myosin motor-like domain in Wangiella (Exophiala) RT dermatitidis."; RL FEMS Microbiol. Lett. 276:99-105(2007). RN [4] RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND ZYMOGEN. RX PubMed=19431044; DOI=10.1080/10826060902953244; RA Abramczyk D., Szaniszlo P.J.; RT "Immunoaffinity purification of the class V chitin synthase of Wangiella RT (Exophiala) dermatitidis."; RL Prep. Biochem. Biotechnol. 39:277-288(2009). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=18992354; DOI=10.1016/j.fgb.2008.10.004; RA Abramczyk D., Park C., Szaniszlo P.J.; RT "Cytolocalization of the class V chitin synthase in the yeast, hyphal and RT sclerotic morphotypes of Wangiella (Exophiala) dermatitidis."; RL Fungal Genet. Biol. 46:28-41(2009). 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 (PubMed:19431044). CHS5 is CC required for the sustained growth at 37 degrees Celsius and is of CC critical importance for virulence (PubMed:14871935, PubMed:18992354). CC Especially important at infection temperatures for maintaining the cell CC wall integrity of developing yeast buds, elongating tips of hyphae, and CC random sites of expansion in sclerotic forms (PubMed:18992354). CC {ECO:0000269|PubMed:14871935, ECO:0000269|PubMed:18992354, CC ECO:0000269|PubMed:19431044}. 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) + UDP + CC H(+); 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 Evidence={ECO:0000269|PubMed:18992354, ECO:0000269|PubMed:19431044}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16638; CC Evidence={ECO:0000269|PubMed:18992354, ECO:0000269|PubMed:19431044}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18992354, CC ECO:0000269|PubMed:19431044}; Multi-pass membrane protein. Membrane CC {ECO:0000255}. Note=Localizes to the regions of cell wall growth in an CC actin-dependent fashion. {ECO:0000269|PubMed:18992354}. CC -!- INDUCTION: The expression level increases quickly and almost doubles CC when cells were shifted to 37 degrees Celsius, compared to cells CC maintained at 25 degrees Celsius (PubMed:12213927, PubMed:14871935, CC PubMed:17937668). Expression is also increased under additional stress CC conditions that are known to initiate development of the sclerotic CC morphology (acidic conditions or Ca(2+) limitation induced by EGTA) or CC of hyphae (induced by nitrogen limitation) (PubMed:14871935). At least CC one negative regulator binding sequence exists in the promoter between CC -880 and -680 bp and another regulatory binding site is localized CC between bp -680 and -450 bp (PubMed:14871935). CC {ECO:0000269|PubMed:12213927, ECO:0000269|PubMed:14871935, CC ECO:0000269|PubMed:17937668}. CC -!- DOMAIN: Contains an N-terminal myosin motor-like domain with a P-loop CC (MMD) that is involved in the actin-dependent localization to the CC regions of cell wall growth. {ECO:0000269|PubMed:18992354}. CC -!- PTM: Maximal activity requires trypsin activation, suggesting a CC zymogenic nature. {ECO:0000269|PubMed:19431044}. CC -!- DISRUPTION PHENOTYPE: Leads to hyperpigmentation and loss of viability CC in stationary phase at 37 degrees Celsius (PubMed:14871935). Reduces CC the virulence in a mouse model of acute infection (PubMed:14871935). CC Causes cell wall integrity defects and subsequent abnormal yeast CC morphology at 37 degrees Celsius (PubMed:14871935). Does dot lead to CC compensation by increased expression of another chitin synthase genes CC (PubMed:12213927). {ECO:0000269|PubMed:12213927, CC ECO:0000269|PubMed:14871935}. CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the chitin synthase CC family. Class V subfamily. {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; AF469116; AAL79830.2; -; Genomic_DNA. DR CAZy; GT2; Glycosyltransferase Family 2. DR VEuPathDB; FungiDB:HMPREF1120_08776; -. DR BRENDA; 2.4.1.16; 6682. DR PHI-base; PHI:390; -. DR GO; GO:0030428; C:cell septum; IEA:TreeGrafter. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC. DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule. DR GO; GO:0048315; P:conidium formation; IEA:UniProt. DR CDD; cd14879; MYSc_Myo17; 1. DR FunFam; 1.10.10.60:FF:000337; Chitin synthase 8; 1. DR FunFam; 1.10.10.820:FF:000012; Chitin synthase ChsE; 1. DR FunFam; 1.20.58.530:FF:000017; Chitin synthase ChsE; 1. DR FunFam; 3.10.120.10:FF:000019; Chitin synthase ChsE; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR InterPro; IPR004835; Chitin_synth. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf. DR InterPro; IPR014876; DEK_C. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR036037; MYSc_Myo17. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1. DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1. DR Pfam; PF03142; Chitin_synth_2; 1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF08766; DEK_C; 1. DR Pfam; PF00063; Myosin_head; 1. DR SMART; SM01117; Cyt-b5; 2. DR SMART; SM00242; MYSc; 1. DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1. DR SUPFAM; SSF109715; DEK C-terminal domain; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS51998; DEK_C; 1. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. PE 1: Evidence at protein level; KW Actin-binding; ATP-binding; Cell membrane; Glycoprotein; KW Glycosyltransferase; Membrane; Motor protein; Myosin; Nucleotide-binding; KW Transferase; Transmembrane; Transmembrane helix; Virulence; Zymogen. FT CHAIN 1..1885 FT /note="Chitin synthase 5" FT /id="PRO_0000460790" FT TRANSMEM 894..914 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 929..949 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1205..1225 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1599..1619 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1626..1646 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1653..1673 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 1..789 FT /note="Myosin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT DOMAIN 957..1016 FT /note="Cytochrome b5 heme-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT DOMAIN 1827..1882 FT /note="DEK-C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342" FT REGION 601..649 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 666..690 FT /note="Actin-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT REGION 794..817 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 607..647 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 99..106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT CARBOHYD 219 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 429 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 668 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1043 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1068 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1462 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1568 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1759 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1790 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" SQ SEQUENCE 1885 AA; 208884 MW; 455A842ED0D426F3 CRC64; MATRGNVPAH MQASLPALPA HLQSDTHITA HLASRFHVSL PTARLSSQGL ICLNTFTSST RGPNGDKEGS AMGEPEDLAR RAWARLGNRA EDQAFGFFGE SGSGKTTVRS HLLSSFLSFS STPLSSKLSL AAFVFDTLTT TKTTTTQTAS KAGLFYELQY DASSNNPTLI GGKLLDHRFE RSRISHVPTG ERSFHVLYYL LAGTSAAEKS HLGLDGHVNI TTAGTGLSRS ASVSHKRWRY LGHPTQMKVG INDAEGFQHF KNALRKLEFP RTEIAEICQV LAAILHIGQL EFGTGQATLT AAEESGGYSH EGGETVTVVK NRDTLAIVAA FLGLGVQDLE ESLRYKTRTI HRERVTVMLD TKGARENADE LATTLYSLLV TYIIESINQR VCAAEDSVAN TISIVDFPGF ADHSSTGSVL DQLLNNAANE SLYNTCLHSI FEKTAEMLES EEVSVPATSY FDNSDAVRGL LKHGNGLLAI LDDQTRRGRT DVQFLESLRK RFENKNKAIT VGSATSTMPG SNFATTNLAA SFTVRHYAGE VDYPVHSLVE ENGDVVSGDL MNMIKATKSD FVANLFGQEA LNTVSHPAEK TAIVQAQVSS KPLRMPSVSR KKHDQLRRMA SRRADRSPAP QEEEPLPGTE EAKVRRTKPT ATGLTQGAAA QFLSALDNIT KSLTAPNVNN YFVFCLKPND RRIANQFDSK CVRQQVQMFG IAEISQRLRT ADFTIFLPFG EFLGLTNADG GVVGSDREKA QLVLDSKHWP PNEARIGNTG VFLSERCWAS IALTGSQAAA YFGGDIGSPS RPDTPGHNPF SDSKARLVGS ADGTPGSFYG DEAKGGGYFG SRELDAKSDA GASAFHSGDM FRNLETKEEL AEKGNKKKVE EVDVVPVSSS RKRWLAIVYF LTWYLPDFAI KWIGGMKRKD VRTAWREKFA INLLIWLSCG LVVFFIIVFP ELICPKQNVY SAAELSAHDG KGKHSAYVAI RGQVFDLGAF MPNHYPKIIP QSSLKKYAGV DATGLFPVQV SALCQGKDGR VDPTVQLDYT ATNISGTAAV ISSTDANRKY HDFRYFTNDS RPDWFYEQMI MLKANYRKGS IGYTPQYVKT LAKKSKSIAI LNDRVYDFTT YNEGGRSVRA PPGEEVPSGV DTDFMDSLVV DLFTQRAGHD VTKYWNALPL DPGLRSRMQL CLDNLFFVGV TDTRNSPRCL FARYILLAVS ILLCSVIGFK FFAALQFGGK NVPENLDKFV ICQVPAYTED EDSLRRAIDS AARMRYDDKR KLLIVVCDGM IIGQGNDRPT PRIVLDILGV SETVDPEPLS FESLGEGMKQ HNMGKVYSGL YEVQGHIVPF MVVVKVGKPS EVSRPGNRGK RDSQMVIMRF LHRVHYNLPM SPLELEMHHQ IRNIIGVNPT FYEFMLQIDA DTVVAPDSAT RMVSAFLRDT RLIGVCGETS LSNAKSSFIT MMQVYEYYIS HNLTKAFESL FGSVTCVPGC FTMYRIRAAE TGKPLFVSKE IIQDYSEIRV DTLHMKNLLH LGEDRYLTTL LLKYHSKYKT KYIFHAHAWT IAPDSWKVFM SQRRRWINST VHNLIELIPL QQLCGFCCFS MRFVVFLDLL STVVAPVTVA YIAYLIVLLA TESDVVPLTA FILLGAIYGL QAIIFILRRK WEMIGWMIVY ILAMPVFSLG LPLYAFWHMD DFSWGNTRLV RGEHGKQILL SDEGKFGPDS IPKKKWEEYQ AELWDAQTQR DDARSELSGY SYGTKSYLPT GSVYGGGYND TQHLMMAPSR SASQLDMHPT PMYGGGGGHN QSRMSLAPSE MLGSQSNLMM PSGRSVADME MSDLTGLPTD DMLLNEIRDI LRTADLMTVT KKGIKQELER RFNVNLDMKR AYIGSATEAI LSGQL //