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Database: UniProt
Entry: H2AX84_KAZAF
LinkDB: H2AX84_KAZAF
Original site: H2AX84_KAZAF 
ID   H2AX84_KAZAF            Unreviewed;       220 AA.
AC   H2AX84;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   04-NOV-2026, entry version 50.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCF58984.1};
GN   Name=KAFR0F03880 {ECO:0000313|EMBL:CCF58984.1};
GN   ORFNames=KAFR_0F03880 {ECO:0000313|EMBL:CCF58984.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58984.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF58984.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., Oheigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; HE650826; CCF58984.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2AX84; -.
DR   STRING; 1071382.H2AX84; -.
DR   KEGG; kaf:KAFR_0F03880; -.
DR   eggNOG; KOG3319; Eukaryota.
DR   HOGENOM; CLU_072117_2_1_1; -.
DR   InParanoid; H2AX84; -.
DR   OMA; AAWCFSQ; -.
DR   OrthoDB; 1932233at2759; -.
DR   Proteomes; UP000005220; Chromosome 6.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0017059; C:serine palmitoyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0090156; P:intracellular sphingolipid homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR   InterPro; IPR007203; ORMDL.
DR   PANTHER; PTHR12665; ORMDL PROTEINS; 1.
DR   Pfam; PF04061; ORMDL; 1.
DR   PIRSF; PIRSF018147; ORMDL; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        83..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..24
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   220 AA;  25273 MW;  4F3B7BD7F75AFA72 CRC64;
     MNERISRTRT NTNSSSLSRS RANSYLTRSR TNSNKSMAEP FKDHRRKRSS SIISHVEQES
     MEDINDQNLL PNMNATWVDQ RGAWIIHIVI IILLKLFFNL LPGITNESAW SLTNTIYVIG
     SYIMFHLIKG TPFDFNGGAY DNLTMWEQID DETLYTPTRK FLIILPIILL LISNHYAKFS
     YNLFTMNSLI ILFLGVVPKL PSTHRLRIQI PGLIGPAQIT
//
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