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Database: UniProt
Entry: A0A2G4T2V2_RHIZD
LinkDB: A0A2G4T2V2_RHIZD
Original site: A0A2G4T2V2_RHIZD 
ID   A0A2G4T2V2_RHIZD        Unreviewed;      1230 AA.
AC   A0A2G4T2V2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:PHZ15350.1};
GN   ORFNames=RHIMIDRAFT_311416 {ECO:0000313|EMBL:PHZ15350.1};
OS   Rhizopus microsporus ATCC 52813.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ15350.1, ECO:0000313|Proteomes:UP000242254};
RN   [1] {ECO:0000313|EMBL:PHZ15350.1, ECO:0000313|Proteomes:UP000242254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ15350.1,
RC   ECO:0000313|Proteomes:UP000242254};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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; KZ303844; PHZ15350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4T2V2; -.
DR   STRING; 1340429.A0A2G4T2V2; -.
DR   OrthoDB; 366603at2759; -.
DR   Proteomes; UP000242254; 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   PANTHER; PTHR13018:SF83; CALCIUM PERMEABLE STRESS-GATED CATION CHANNEL 1; 1.
DR   PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR   Pfam; PF14703; PHM7_cyt; 1.
DR   Pfam; PF02714; RSN1_7TM; 2.
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:UP000242254};
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        88..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        509..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        555..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        620..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        663..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        712..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        737..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        776..796
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..233
FT                   /note="CSC1/OSCA1-like N-terminal transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF13967"
FT   DOMAIN          255..495
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          507..590
FT                   /note="CSC1/OSCA1-like 7TM region"
FT                   /evidence="ECO:0000259|Pfam:PF02714"
FT   DOMAIN          595..797
FT                   /note="CSC1/OSCA1-like 7TM region"
FT                   /evidence="ECO:0000259|Pfam:PF02714"
FT   REGION          351..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..865
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1061
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1096
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1131..1151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1230 AA;  138477 MW;  A3820217C32848A2 CRC64;
     MSLTASVTGP SPTSFIPSTT SSIYSIPTSL SSVNGSSIIT SSPTVFTSTN NTIPTSTITT
     ATSTTTPGSI FPGGEKFFNT QNPSKPSIQF GICAVAGLVF FIAFCFLRVR LPVMFAPRKN
     MKRHKPPELS NSFFGWIIPV LKASTEEMLL NVGLDAVLML HFLVMAMKIF GLCSIFGVIV
     LIPISATAKN NEKSMSDIEK ISITHTEDGD LRLIAFLVFT YFVTIVTLYY LTQSYYNYVY
     LHAKYMLNQS KQMVSRSVII TGIPERLRSD QALAEYYENL GIGPVESCYV VRTVHQLDKL
     IKQRASALTK LEKAYAKYWG NPCRIPGYDP DIILDDVEMY KKVLDLAEKR NDSSSSSSDS
     EVEDENGNKQ KKKPFALRLT KKNTWKRAVN TTFFKGLIDP LEQEKRSKRP TVRTGFLGLF
     GQKIDAIEYY TVLFDNLDKM VAEKRRSPHY EMTNVAFVTF EHMSSAVIAS QIAIHPEPFA
     CRTILAYEPR DVLWSSVAIR GRERIIREII VWAITIALVI FWFVPVTILS SLLSLETLKR
     VIPKLAKAIE GNEALKGFVS SFVTTVALNI VTSVLPLIFD GRVITKTQAQ QTNKMIIIAL
     GYYQGLRSRS AIAESTFSKY FFFLVFFTLI TFTLANASMQ TVIDFANNPT SIPERLADTL
     PNIAPFFINY VILQGFLLMP MNLLLLGALI VRGFYHAFIC KTPRDHAENR APWSFNYGTG
     YPVPLLVFII VLEYSCISPI IMVFGAIYFC FTYVVYKYQF LYVYFRPYEA AGRLWIMTVP
     RIIFGLVLFQ LTMTGYFVLR KFIALGATCA PLIAITILYK FILDRAFLKN ARNLPMQLLR
     DNMQKLPDVV DPSDDDDDDD DDDDNYTQQQ QLKEADHSKN KNNDTTGTNS TEKVDREKQM
     VRNKWKTAAL SAVQLRVKPK EEEQTSPEAS AVSIVRPRHR KVVLDEDDYE AVPDKLTDYR
     QPPMQLNPGL LDTGLKRYGN PWIVGILPQL WLPMKEPDKA HKEGKAQSKR KRASDAFNRR
     SEGGGTLAQH LAEVLRRMEM EAKRKEKKPD EKNEDDNKSS SGQDNQQRTK IAQETAQMTA
     ASLAGHSPNN KTSALRTLFK MGALKKQGPK ATADAQIDEV AMSPVEPQHQ DPLEALEKGS
     PVRHDSSESK ASAAKSVHAT YYHHPERRRH HSENTAHATP SRPEAHHSGV SSPAAFHDES
     LTDDEHVEDH GEERLPTKRL SSVPLIDRSK
//
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