ZONAD_KOMPC
ID ZONAD_KOMPC Reviewed; 587 AA.
AC F2QXM5;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Putative adhesin {ECO:0000305};
DE AltName: Full=Zonadhesin {ECO:0000303|PubMed:27313058};
DE Flags: Precursor;
GN OrderedLocusNames=PP7435_Chr3-1213;
OS Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL
OS Y-11430 / Wegner 21-1) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=981350;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=21575661; DOI=10.1016/j.jbiotec.2011.04.014;
RA Kueberl A., Schneider J., Thallinger G.G., Anderl I., Wibberg D., Hajek T.,
RA Jaenicke S., Brinkrolf K., Goesmann A., Szczepanowski R., Puehler A.,
RA Schwab H., Glieder A., Pichler H.;
RT "High-quality genome sequence of Pichia pastoris CBS7435.";
RL J. Biotechnol. 154:312-320(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=27388471; DOI=10.1093/femsyr/fow051;
RA Valli M., Tatto N.E., Peymann A., Gruber C., Landes N., Ekker H.,
RA Thallinger G.G., Mattanovich D., Gasser B., Graf A.B.;
RT "Curation of the genome annotation of Pichia pastoris (Komagataella
RT phaffii) CBS7435 from gene level to protein function.";
RL FEMS Yeast Res. 16:0-0(2016).
RN [3] {ECO:0007744|PDB:5FX8}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-339, PROTEIN SEQUENCE OF 20-32
RP AND 216-233, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BONDS.
RX PubMed=27313058; DOI=10.1194/jlr.m069617;
RA Chen Y., Wennman A., Karkehabadi S., Engstroem A., Oliw E.H.;
RT "Crystal structure of linoleate 13R-manganese lipoxygenase in complex with
RT an adhesion protein.";
RL J. Lipid Res. 57:1574-1588(2016).
CC -!- FUNCTION: Putative adhesion protein. May be involved in cell-cell
CC interaction, interacting with other proteins by salt bridges and
CC hydrogen bonds. {ECO:0000305|PubMed:27313058}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000255}. Secreted, cell wall {ECO:0000305}. Note=Identified as
CC covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer
CC cell wall layer. {ECO:0000305}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC {ECO:0000305}.
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DR EMBL; FR839630; CCA40153.1; -; Genomic_DNA.
DR PDB; 5FX8; X-ray; 2.60 A; U=20-339.
DR PDBsum; 5FX8; -.
DR AlphaFoldDB; F2QXM5; -.
DR SMR; F2QXM5; -.
DR EnsemblFungi; CCA40153; CCA40153; PP7435_CHR3-1213.
DR HOGENOM; CLU_464686_0_0_1; -.
DR Proteomes; UP000006853; Chromosome 3.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:27313058"
FT CHAIN 20..562
FT /note="Putative adhesin"
FT /id="PRO_0000447318"
FT PROPEP 563..587
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000447319"
FT REPEAT 432..455
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 466..489
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 491..512
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 513..531
FT /note="4"
FT /evidence="ECO:0000305"
FT REGION 432..531
FT /note="4 X 24 AA approximate tandem repeats, Thr-rich"
FT /evidence="ECO:0000305"
FT LIPID 562
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 211..261
FT /evidence="ECO:0007744|PDB:5FX8"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:5FX8"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5FX8"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 120..133
FT /evidence="ECO:0007829|PDB:5FX8"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 194..206
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 294..305
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:5FX8"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:5FX8"
SQ SEQUENCE 587 AA; 62905 MW; 0FDC8E4D82E4B790 CRC64;
MKFAISTLLI ILQAAAVFAA FPISDITVVS ERTDASTAYL SDWFVVSFVF STAGSDETIA
GDATIEVSIP NELEFVQYPD SVDPSVSEFF TTAGVQVLST AFDYDSHVLT FTFSDPGQVI
TDLEGVVFFT LKLSEQFTES ASPGQHTFDF ETSDQTYSPS VDLVALDRSQ PIKLSNAVTG
GVEWFVDIPG AFGDITNIDI STVQTPGTFD CSEVKYAVGS SLNEFGDFTP QDRTTFFSNS
SSGEWIPITP ASGLPVESFE CGDGTISLSF AGELADDEVL RVSFLSNLAD DVLEVQNVVN
VDLTTADSRK RALTSFVLDE PFYRASRTDT AAFEAFAAVP ADGDITSTST AITSVTATVT
HTTVTSVCYV CAETPVTVTY TAPVITNPIY YTTKVHVCNV CAETPITYTV TIPCETDEYA
PAKPTGTEGE KIVTVITKEG GDKYTKTYEE VTYTKTYPKG GHEDHIVTVK TKEGGEKVTK
TYEEVTYTKG PEIVTVVTKE GGEKVTTTYH DVPEVVTVIT KEGGEKVTTT YPATYPATYT
EGHSAGVPTS ASTPPQATYT VSEAQVNLGS KSAVGLLAIV PMLFLAI
