ID   KRE6_CANAX              Reviewed;         740 AA.
AC   P87023;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Beta-glucan synthesis-associated protein KRE6;
GN   Name=KRE6;
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: Involved in the synthesis of (1->6)- and (1->3)-beta-D-glucan
CC       polymers of the yeast cell wall in vivo. It is required for full
CC       activity of beta-glucan synthase in vitro. It may be a beta-glucan
CC       synthase, part of a multiprotein glucan synthase or a modulator.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC       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; D88490; BAA19593.1; -; mRNA.
DR   AlphaFoldDB; P87023; -.
DR   SMR; P87023; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PRIDE; P87023; -.
DR   VEuPathDB; FungiDB:C3_05830W_A; -.
DR   VEuPathDB; FungiDB:CAWG_02892; -.
DR   PHI-base; PHI:8716; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; Golgi apparatus; Membrane;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..740
FT                   /note="Beta-glucan synthesis-associated protein KRE6"
FT                   /id="PRO_0000084330"
FT   TOPO_DOM        1..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..740
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          299..694
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        593
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   740 AA;  82457 MW;  9DA0537F0B357840 CRC64;
     MASQRDLTSN NPHFHISSSR NNTNDDFNSD HNPRNPFGDE PEEEEELDSA SFSSSSQNNQ
     PHHPFATSNQ TSSTNNLHST NSIRNEAEYG KPFQAYSGYY SNGGSSSYLN QEGVISDESR
     LLSSGNNNNN NNNNRDVSSV GGGGGSGDNR LNPTSPAEFD RYPSMAGSRV VSSTSLVSFN
     NPSNMMRNHH QHQPHLGSSS SPTSSSMNND SISDKSTSPF PNDFSPFGGY PASSFPLSID
     EKEPDDYLNN PDPVQDAEYE KNRFMHDLKN MDKRSLGGLI GFIILFIAAL AVFIILPALT
     YSGATNPYHP ESYEVLTKYS YPMLSAIRMN LVDPDTPESA YKKKAKDGSE WVLVFSDEFD
     AEGRTFYEGD DQFFTAPDIH YDATKDLEWY DPDAVTTANG TLNLRMDAYK NHNLFYRSGM
     VQSWNQLCYT QGHLEISARL PNYGNVTGLW PGLWSMGNLG RPGYLGSTDG VWPYSYDSCD
     AGITPNQSSP DGISYLPGQR LNKCTCPGEL HPNRGVGRGA PEIDVIEGEV MTDSSGKKEN
     CGVASQSLQL APMDIWYIPD YNWVEIYNFS VSTMNTYTGG PFQQALSATT MLNVTWYEFG
     DNAHNFQTYG YEYLNDPETG YLRWFVGDDP TLTVYSQALH PDGNIGWRPL SKEPMSLILN
     LGISNNWAYI DWPSISFPVT FRIDYVRVYQ PPDQINVGCD PTDFPTYDYI QQHLNLYENA
     NITSFEDGGY KFPKNSLIGC