ID   SKN1_CANAX              Reviewed;         737 AA.
AC   P87024;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Beta-glucan synthesis-associated protein SKN1;
GN   Name=SKN1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9079924; DOI=10.1128/jb.179.7.2363-2372.1997;
RA   Mio T., Yamada-Okabe T., Yabe T., Nakajima T., Arisawa M., Yamada-Okabe H.;
RT   "Isolation of the Candida albicans homologs of Saccharomyces cerevisiae
RT   KRE6 and SKN1: expression and physiological function.";
RL   J. Bacteriol. 179:2363-2372(1997).
CC   -!- FUNCTION: Required for synthesis of the major beta-glucans of the cell
CC       wall. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC   -!- SIMILARITY: Belongs to the SKN1/KRE6 family. {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; D88491; BAA19594.1; -; mRNA.
DR   AlphaFoldDB; P87024; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PRIDE; P87024; -.
DR   CGD; CAL0000200054; SKN1.
DR   VEuPathDB; FungiDB:C3_05810C_A; -.
DR   VEuPathDB; FungiDB:CAWG_02891; -.
DR   OMA; RIDYIRI; -.
DR   PhylomeDB; P87024; -.
DR   PHI-base; PHI:8715; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:UniProt.
DR   CDD; cd02180; GH16_fungal_KRE6_glucanase; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR005629; Skn1/Kre6/Sbg1.
DR   PANTHER; PTHR31361; PTHR31361; 1.
DR   Pfam; PF03935; SKN1_KRE6_Sbg1; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycoprotein; Membrane; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..737
FT                   /note="Beta-glucan synthesis-associated protein SKN1"
FT                   /id="PRO_0000097779"
FT   TOPO_DOM        1..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..737
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          348..691
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          1..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        590
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        718
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   737 AA;  83708 MW;  E2850C1142F86C76 CRC64;
     MERDLTYNAP KIKFTDTEGQ EEHFYFNRSN NSTNDLTSHD SSSTQLQDAN SRRQAPPPPP
     HNPFSDNSHE NSTESLYQSE TRFHQPLLHN DSNNSNSSIG NNRQRIPSQQ HDTSSLYSAS
     PISTSPLVSN FQSYSDNQDE MTRGKYNQNT NRSSSNYIQH SPTSAGYDRY PLKTQSSIGG
     SMSRIGLSSS SPSQQQQQHM YDNNSSNRSS YSPDSATDLM VYENGEFSPF GGYPASLFPL
     SIDEKEPDDY LHNPDPVQDA EYDKNRFLYD LKTMDKKSMN GLIAFIVMFL IAIAIFIILP
     VFTYTGYNPK AKNFENYEVL TRYSYPRLSA IRTSLIDPDT PEDALFWKSK NGEEWPLVFS
     DEFNAEGRTF YEGDDQFFTA PDLHYDATKD LEWYDPDAVT TANGTLTLRM DAFKNHGLFY
     RSGMIQSWNQ MCFTQGKLEF SAKLPGYGNI TGFWPGLWSM GNLGRPGYLA STEGVWPYTY
     DSCDAGITPN QSSPDGISYL PGQRLNKCTC PGEAHPNRGV GRGAPEIDAL EGEIHGVIGR
     VSQSLQVAPY DIWYMPNYDF LEIHNSSITL MNTYAGGPFQ QAISGVTMLN VTWYEYGDHQ
     HNFQKYGYEY LNDDESGYLR WFVGDNPTFT IYSQALHPNG NVGWRKLPKE PLSLILNFGI
     SNNWAYIDWP SLVFPSTMRV DYVRVYQPKD QINVGCDPTD FPTYDYIQQH LNVYQNVNLT
     KFEDGGYTFP KHKLIGC