ID A8PVN0_MALGO Unreviewed; 885 AA.
AC A8PVN0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=DUF221-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGL_0912 {ECO:0000313|EMBL:EDP44430.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44430.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44430.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.
CC {ECO:0000256|ARBA:ARBA00007779}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP44430.1}.
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DR EMBL; AAYY01000003; EDP44430.1; -; Genomic_DNA.
DR RefSeq; XP_001731644.1; XM_001731592.1.
DR AlphaFoldDB; A8PVN0; -.
DR GeneID; 5855950; -.
DR KEGG; mgl:MGL_0912; -.
DR VEuPathDB; FungiDB:MGL_0912; -.
DR InParanoid; A8PVN0; -.
DR OMA; ATIIFHI; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005227; F:calcium activated cation channel activity; IEA:InterPro.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR InterPro; IPR032880; Csc1/OSCA1-like_N.
DR InterPro; IPR022257; PHM7_ext.
DR PANTHER; PTHR13018:SF143; -; 1.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF12621; PHM7_ext; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..885
FT /note="DUF221-domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002727968"
FT TRANSMEM 31..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 568..595
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..194
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 220..412
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 426..699
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 810..875
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
SQ SEQUENCE 885 AA; 100811 MW; 76CADDDF4220C548 CRC64;
MIKQRNALIL ILSCLALPVL AAEDDEMRDS STSSIISAIV YALILAGIFM VVFLYLRPRY
PAIYQPKTYR ALPASRNTQP LPKGTFNWIP SFLSVPDHEI LRINGLDAYS FIWFIVLMLR
IFVPIWILSW IVLMPLYAAD LPVNSGSDPV GRGKGFNMFT FGNVINENNQ QQKRSAGVLI
LHYIFMAWFI FNIHDVMTHF IKLRKEFLTS PDHRNTNQAK TFLVTSVPNQ YLSETKIKQL
YENLPGGIKR VWINRNLKEL PKLVENRDKL ANKLEGAVSK LIATAAKKVK KGKVEAVALP
EGSEPSLDVA DRYVPEKKRP KHRLGKIPCI GEKVDTINYS REELPRMNRE IEDIRQNVIN
DYETYPPESS AFVLCNTMQG AYTGASFRPV ENKSQMDKSY VEVHPDDIVW ENMSFNPYER
KLRTCACWGV TWLTVIFWAI PVALVSLFSN VDYMSEKIGF LGWIKQIPSV PLGIIKGVLP
TTALAILNSL LPPWLRFHAR MSGVPTRNLI ELSLMTRFFI FMIVQNFIIL TVLAGIQQNL
DAFWDDVKEP KKFVQDISSA IPRASSFYLS YMALIGLSAS AGIFSQLIPL LLYYVKIRFL
SSTPRKLWHL RNDFNSPPWG TLYPSTLFMT VIAFGYMVLQ PVTNGFACVA FFLLYLAYRY
SYLYVFDCKP VKETAGQFFV KAIHFTFISA YVSIFVVALM YFFKTGDNAS FAAMGVLTIV
LGLLVAAYHI YMYVWYEREM QKIPELLASK TNELSSNPLN DGAGALVLPE KDEYYANAEQ
EKQLIPQGPR PLGPESKALA LQMEDPGLEE EKQQMREIET MNAFFNPARL KDQMILWYPN
DNYGIGRSQM LADYSAGYQS SVDNAFINEK YKIDENADVP PGEKK
//