CHS5_CANAL
ID CHS5_CANAL Reviewed; 562 AA.
AC O74161; A0A1D8PH26; Q5AHI9; Q5AHW5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Chitin biosynthesis protein CHS5;
GN Name=CHS5; OrderedLocusNames=CAALFM_C204140WA;
GN ORFNames=CaO19.807, CaO19.8426;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060;
RA Ohta A., Sudoh M.;
RT "Candida albicans CHS5.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Involved in chitin synthesis and also required for mating.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CHS5 family. {ECO:0000305}.
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DR EMBL; AB012123; BAA32787.1; -; Genomic_DNA.
DR EMBL; CP017624; AOW27440.1; -; Genomic_DNA.
DR RefSeq; XP_720931.1; XM_715838.1.
DR AlphaFoldDB; O74161; -.
DR SMR; O74161; -.
DR STRING; 237561.O74161; -.
DR PRIDE; O74161; -.
DR GeneID; 3637333; -.
DR KEGG; cal:CAALFM_C204140WA; -.
DR CGD; CAL0000186466; CHS5.
DR VEuPathDB; FungiDB:C2_04140W_A; -.
DR eggNOG; KOG1181; Eukaryota.
DR HOGENOM; CLU_019904_3_2_1; -.
DR InParanoid; O74161; -.
DR OrthoDB; 1141896at2759; -.
DR PRO; PR:O74161; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0034044; C:exomer complex; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000747; P:conjugation with cellular fusion; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR CDD; cd13945; Chs5_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031673; Chs5_N.
DR InterPro; IPR031669; Fn3_2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16892; CHS5_N; 1.
DR Pfam; PF16893; fn3_2; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Golgi apparatus; Reference proteome.
FT CHAIN 1..562
FT /note="Chitin biosynthesis protein CHS5"
FT /id="PRO_0000089659"
FT DOMAIN 78..170
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 164..259
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 283..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 333
FT /note="I -> T (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="V -> A (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="A -> V (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="E -> G (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..453
FT /note="IREQVNST -> TRKQSNNA (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="R -> T (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="N -> D (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="V -> I (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="A -> V (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
FT CONFLICT 533..535
FT /note="KTS -> ETP (in Ref. 1; BAA32787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 62158 MW; 2831E230DD655809 CRC64;
MVEVSLTVGK LDASLALLLT KDHHLIEFPT ILLPNGVRAG SIIKIRCDQD FDSEKEEAEK
FTKIQDEILQ TFATNLPQPP NLKIKNVTQT SCVLEWDKLN LGTATLKNLI LFKDGKKLGS
IPQPLNNRTS KLSGLPIDKS FKVQLRLDTT AGTFLSNEIE VTTHKMTDLS GITVCLGDLT
PNDQFNKEDI EEALKNMGAK YPVQQQVKVD TTHFLCTREN KQNPEYVKAN DMNIPIIRPE
WLKACERERR IVGVRDFYVK DCVLPDIFAK NYWQKTTSQT AGNFSAQSLP KESPAVPDKE
GLPKTDLNKE SVKDEPTEVD HAKEDSVTQE PAIEEISAVV SENIITPDIA NEETDIVEGE
STKIESVPTD EIDTKVESTP VAVETEDVVA ESPADQDAAV TLEPTSVDDQ ELHQSDETLK
QVNDGQQEID VGDATEQPEK EEIDDIREQV NSTVNNTERQ ETATDDAFDT VPLEGDENIA
TAAKETEPTS TEPTESVNVT NVNNSASEEA GKDDNDDEDD EDEDADNEGK SNKTSEQSSE
GSATGSPSKK KNKKKKKNNK KK
