ID G8BMN4_TETPH Unreviewed; 1016 AA.
AC G8BMN4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DUF221 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TPHA0A00770 {ECO:0000313|EMBL:CCE61162.1};
GN OrderedLocusNames=TPHA_0A00770 {ECO:0000313|EMBL:CCE61162.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE61162.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE61162.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
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}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.
CC {ECO:0000256|ARBA:ARBA00007779}.
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DR EMBL; HE612856; CCE61162.1; -; Genomic_DNA.
DR RefSeq; XP_003683596.1; XM_003683548.1.
DR AlphaFoldDB; G8BMN4; -.
DR GeneID; 11532794; -.
DR KEGG; tpf:TPHA_0A00770; -.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_2_1_1; -.
DR OMA; NWACVAL; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000005666; Chromosome 1.
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; PHOSPHATE METABOLISM PROTEIN 7; 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:UP000005666};
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 TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..161
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 184..378
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 390..662
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 917..1009
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 757..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 116887 MW; 8D429F7CFEABC830 CRC64;
MPASSSSTSA FVTSLIFNGI IALIFIILFI NLRPKFTRVY EPRSLKDIYT IKEEERTEPA
PYGYFKWVPF LLTKRHSYLI QNASVDGYFF LRYLAIILLI SFLSFFVLFP ILLPVNATNG
RDYKGFELLS MSNVTNKNRF YAHVFLSWIW FSIIIYIIYR ELYYYVVFRH ALQTSPLYDG
LLSSRTIILT DLNPSKNSEL ERIFTKANKI SVAKNVKELE KLCKERKSDT QRYESALNKM
IKQSMKKKLK ADKNKKYHDK LYENDRRLVN DLETYVPYEK RPKHYIGSKL PSFLKMINGK
KVNTVSYLNE HIPEENEQIF TKQQEYEHSR EYLRTVFIQF DTQLEAQKVY QTLDYLLGRE
NYAKKYIGYS PEQIVWSNLN MTTRERSWKR CLATTFLVLM IIFWAIPVAV VGMISNISFL
TTKIFFLEFI NNLPNFLLGL ITGILPSVAL SILMSLVPPV IMYVGKLRGL TTLKHIDLYC
HSWYFAFQVI ETFIVTTGTS SASSTVTAII DDPSQAMTLL SNNLPKASNF YISYFLLLGL
TVPTGMLLQI ITLVMSKIKG MLFTSTPRQK WTSYNTLATP SMGILYPTIE IIMVILISYS
IIAPLVLVFS TLALFLLYLA YVYNLNFVMG FSLDSKGRNY PKGLFHIFVG IYMSEVCLIG
LFVMLKSWGC VVLEAFYLGI TALLHIWFKR KFIPLFDIVP LSAIYLSRGL PNYQYPNEDL
GTKEVHDLRE RVKQALESDE TGGVLRLATD HELKVANILK TEERNPDESS PSSGENTLSE
SNPSSILNGG EKKIIETEHL ENANGSSDID VDNRRNNNTD LPAHDGSEVE DKDASSKTGT
TFVKGDETFR KLHYEDLEGL ERPVLGNQGG EKHKSTVMHN TDVGIVYTDK TAMTRELEAL
PENINRSFTW KQRLKNFFHP SQAYKFETMR KRLPHVFNTT IAYSNKFISQ AYINPCVSDE
NPKIWICKDT MGVSQQQIEE ANNYNLYVTD AFTSFDKKGR AQFTFNPPDF LFEGKK
//
