CHS8_USTMA
ID CHS8_USTMA Reviewed; 2005 AA.
AC Q4P9K9; A0A0D1E236;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chitin synthase 8;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 8;
DE AltName: Full=Myosin chitin synthase 1;
GN Name=CHS8; Synonyms=MCS1; ORFNames=UMAG_03204;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=17042749; DOI=10.1111/j.1567-1364.2006.00133.x;
RA Ruiz-Herrera J., Xoconostle-Cazares B., Reynaga-Pena C.G., Leon-Ramirez C.,
RA Carabez-Trejo A.;
RT "Immunolocalization of chitin synthases in the phytopathogenic dimorphic
RT fungus Ustilago maydis.";
RL FEMS Yeast Res. 6:999-1009(2006).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16314447; DOI=10.1105/tpc.105.037341;
RA Weber I., Assmann D., Thines E., Steinberg G.;
RT "Polar localizing class V myosin chitin synthases are essential during
RT early plant infection in the plant pathogenic fungus Ustilago maydis.";
RL Plant Cell 18:225-242(2006).
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 (Probable). Involved in
CC mating tube and dikaryotic hyphae formation and required for the
CC formation of invading hyphae during plant infection (PubMed:16314447).
CC {ECO:0000269|PubMed:16314447, 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:0000269|PubMed:16314447};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:17042749}; Multi-pass membrane protein
CC {ECO:0000255}. Note=A constitutive cytoplasmic pool is present that
CC localizes to intracellular microvesicles termed chitosomes. Chitosomes
CC constitute a separate secretory route distinct from the typical
CC secretory pathway and serve as a vehicle for delivering the enzyme to
CC the sites on the cell surface where polysaccharide sythesis takes
CC place. Localizes to septa of yeast-like cells and to the basal septum
CC separating the living tip cell from the vacuolated part in hyphae. Also
CC localizes to the growing bud tip in yeast-like cells and in a tip-ward
CC gradient at the hyphal apex. {ECO:0000269|PubMed:16314447,
CC ECO:0000269|PubMed:17042749}.
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}.
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DR EMBL; CM003147; KIS68630.1; -; Genomic_DNA.
DR RefSeq; XP_011389642.1; XM_011391340.1.
DR AlphaFoldDB; Q4P9K9; -.
DR SMR; Q4P9K9; -.
DR IntAct; Q4P9K9; 1.
DR MINT; Q4P9K9; -.
DR STRING; 5270.UM03204P0; -.
DR PRIDE; Q4P9K9; -.
DR EnsemblFungi; KIS68630; KIS68630; UMAG_03204.
DR GeneID; 23563730; -.
DR KEGG; uma:UMAG_03204; -.
DR VEuPathDB; FungiDB:UMAG_03204; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_2_1; -.
DR InParanoid; Q4P9K9; -.
DR OMA; MRYDDKR; -.
DR OrthoDB; 20724at2759; -.
DR BRENDA; 2.4.1.16; 6587.
DR PHI-base; PHI:1114; -.
DR PHI-base; PHI:2226; -.
DR Proteomes; UP000000561; Chromosome 8.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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-KW.
DR GO; GO:0004100; F:chitin synthase activity; IBA:GO_Central.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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 CDD; cd14879; MYSc_Myo17; 1.
DR Gene3D; 3.40.850.10; -; 2.
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; PTHR22914; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01117; Cyt-b5; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Cell membrane;
KW Cell wall biogenesis/degradation; Cytoplasmic vesicle; Glycoprotein;
KW Glycosyltransferase; Membrane; Motor protein; Myosin; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2005
FT /note="Chitin synthase 8"
FT /id="PRO_0000270624"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 965..985
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1232..1252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1604..1624
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 TRANSMEM 1680..1700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..773
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1948..2003
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT REGION 585..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..669
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1796..1821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2005 AA; 222618 MW; EAB6EA732428DA10 CRC64;
MSALDEVAKL SQLTNITPDT IFSVLRDRFY AGLPYTALSD SILVSVNPYA SSGNRNSDDT
LREYTSDYRQ TNKQLRAATL PPHIFAHACN AYFYMRRTGQ DQSLLMAGDT SSGKSEVRRL
ALRALIDLSV APPGKKGSKL GVQIPSAEYI LEALGNSRTL ENSNASRFGK YTELQFSDSG
KLVGAKTLDY YLEKNRVVSA ASSERNFHIF HYMVAGASDE EKQYLGIHDA ASFRYLGQAS
RNMDTQDAAK FDRLKLAFKN VGFSKRNVAS ICQVLAAILH LGNIEFHYDR QRTQDSATIR
NPEVLDKVAE YLGISSKSLE EALTYKTKMI RNEVCTILLD ADGASDHRDD LAKSLYSLLF
AWVNESLNEK LCRDDFDTFI GLLDLPGFQN LSKGNSLDQF CVNFACENLH RFMLRSVFEK
RRDEFADEGI SHLSPEVPYF DNAETLRLMT NQPGGLIHIM DDQARRMPKK TDQTMIEAFG
KRWGNHPSFK VGPADRSGFS SFTISHYNSA VTYTSENLLE KNSEVVSTDF VSLLRGNPQE
SGKLRNDSSQ SSGSTIPFIR GIFNTKVLKT QSHPKNDQTI VAAQQSVKPM RAPSTRRPNR
GNTIKRTNTI KKADDDDSDE DAADAADAST SKKNAVRCVA GDFRGALDLL LETLEDTKTW
FTLCLRPNDN QLPNQFEARV VKQQITTLGL SEMSRKLLNE YSVSMTYEEF CQRYADVPSL
QAVQMRDAVS GEAKQKFSAA RQVMSWSDQE AVSGRVKVFL SHTAFRELED ELRAADAEEV
KNNEKRAQLD ADAAARGESD PFSPVAVLAD DYTRSRSNDF VGAYGDPFKE RSSVALPLVG
RGAAGNEDDL EEVKSQYSGM SGTLARHSFV GGLSGAPSFV ASEAYAPSRN MFADMGKNGL
NEKAGTAAFT EEPLGEVAEE VGVSSTRRKW VALTWAITFW IPSFILSRFR SLKRPDIRMA
WREKLAINLI IWFICACAVF VIVVLGNLIC PKQHVYSPTE FASHKGDSSF TAIRGEVFDL
SNLVASHKTI VPVVPANSIL AYAGEDATPI FPVQVNALCN GVDGNVSPWV QLSNENSTDK
HAQYHDFRSY HIDDARPDWY YESMWLLRSN YRVGFMGYTT DGIRDILSEG RAVAIYRGDI
YDVSDYIKQG NQGVLRAPDG FQAPANTNRK FMSDAIISLI AQNPGKDITK QLDNLPLDPV
VLDRQRVCLR NLYFIGKVDH RNSPQCRFAQ YILLALSLFM VAILGFKFLA ALQFGRARKP
EDHDKFVICQ VPCYTEGEES MRKTINSLAA LKYDDKRKLL FIICDGMIVG SGNDRPTPRI
VLDILGADPN LEPEALSFLS LGEGSKQHNM AKIYSGLYEH HGHVVPYIVV VKCGKPSERS
RPGNRGKRDS QLVLMRFLNK VHFGLPMNPM ELEIYHQIKN VIGVNPSFYE YILQVDADTE
VEAMSLNRFI SAFIRDKKVI GLCGETALSN AKASIITMLQ VYEYYISHYL AKAFESLFGS
VTCLPGCFSM FRIRTPDTHR PLFIASQIVE DYAENRVDTL HTKNLLHLGE DRYLTTLVLK
HFGKYKTIFV RDCKAWTVAP DDWKVLLSQR RRWINSTVHN LVELIFTPGL CGFCLFSMRF
IVFIDLLSTI IAPVTVCYIV YLIVLVATAN GTVPLTAIIM LAAIYGCQAV IFLLNRKFEM
IGWMIVYIIG IPIWSLFLPL YSFWHMDDFS WGNTRVVMGE KGQKVVLHEE GTFDPSEIPL
QTWTDYENEL WERNSARSIG SIIEAARAEN KSLGSRAGSQ YAPSLYGQPM LPHNASFGHS
PSPSYGGTPS QFGAFAPGPG SQIGGSQIGA GAGYFPQDAA RQSTYSIGGG YGGQAMSMYG
LPPSSSFGVP TGGSGFMPQP FNTTASMYGY PQQVAATQSI YGGSQLGFGG GFATAEQQQQ
QQQQQQAAGL SGSGGSKSPP REAVAGGLPS DSQIKLDIRS LIAESDLTTI TKKQLRAKLE
QKYATSIESK KAFINSEIEN VLSES
