ID D8U8Q2_VOLCA Unreviewed; 1172 AA.
AC D8U8Q2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=ERD4-related membrane protein {ECO:0000313|EMBL:EFJ43788.1};
GN ORFNames=VOLCADRAFT_95919 {ECO:0000313|EMBL:EFJ43788.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ43788.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
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; GL378369; EFJ43788.1; -; Genomic_DNA.
DR RefSeq; XP_002955034.1; XM_002954988.1.
DR AlphaFoldDB; D8U8Q2; -.
DR GeneID; 9622047; -.
DR KEGG; vcn:VOLCADRAFT_95919; -.
DR eggNOG; KOG1134; Eukaryota.
DR InParanoid; D8U8Q2; -.
DR OrthoDB; 315657at2759; -.
DR Proteomes; UP000001058; 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; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR PANTHER; PTHR13018:SF98; TO DEHYDRATION PROTEIN, PUTATIVE, EXPRESSED-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 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:UP000001058};
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 48..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 726..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..904
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..140
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 463..622
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 636..902
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 214..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 130935 MW; ECB9E76128CF9E5C CRC64;
MCRYAKDIDL KPKRLPNGLL SWIYPVITYP EGDIIDEAGL DCAMYLRILR FGVYLFFPLT
IFCIIVVLPP NMKSNGIEAI LAEQALRNAG KNQTSGKGDL EFSDFDHYSL SNVEAASPKM
WAHLFAVYCV VLYTLWLLWR FNRESVLLRL LFLGNAKRGG PSHTVLVTDI PGISEAVSKA
LRDERAKKQE MKKMERDKSI ISQKSVDVQL DDDSYAELPD QPRTATTSVA STTLKPQTSL
RKGRVVSISE PPVLVVQQQQ LQQQQQQFTP RAVPSVEKGG RSNVSASPFS DASAKSFEST
ADAELPGSST KPEVVELKSA ASASGGAAAG GGPAGPAGGA SFVVKAGGNS RFNLRSILSS
TASDAQYRLV VDDLDPKYAA TGGKLELARV GKTNEEILKE LQVMEKDDLV KGLPEKLGVD
TRPLPPTRRN TKRYEYDLKT TVLDPVHEAL ETLRKGVTPQ QLVAREFALV YGTSNVAAVN
MIQDTSALEP LAEEYNQARV CQDLDDYLEM AKLRLKLRKA LPQKQISILC ARYQDMDYVK
KFKTKWFVKV DAVEFWLERM KYLRERIKIE QAKCVRKMAP SAFVTFNTRM AQAVSANSLH
SHDENAWRVQ NAPAPFEVVW KNLSLTMPIK NGRLYLLWAA FWGMTIFFMV PVSFIQGMIE
VPKLASIPVL GDIVTTPPIK QLLQAVIPGL VLKIFLALVP TILRIMAQLS GATSVSEIDF
GVVKRFFLFQ TVVVFFGSII LGSFFNQLKQ WVKEPSSVIA TLGKSIPMTS TFFITYLLVN
GLGVKSFAFI RLPNFVIYWI LSKFAGSPAA RQRMWMFQWT NNGTTVVDHT IAMMLGLTFS
CINPIVCPAA LAYFLVNFLG ETYNNVYVYR RQYESGGMLW KTVYNQVMVA LYIMQITMLG
LLSLKKFKFS PFMFPLIIFS ITSHISTLQL FNRPWSVTAL HDAAYMDMLE ADQRRMTLLA
AAREERKKKR DKIKRAYDDA VRQAENNDDP PPPYDTRLDE VPSPGYPGAG KAELLLLESI
EGDGYALNSQ EKREVEEMYM NPVFKVKLEE VERLEKLAED VQTRLPRLNE WVAEYKVYRR
EVKKRHIKGD TEQVTPPKMP EDLTIYDADP NLQDSDDEED AGGAAGGNPN STTNNNKNDT
AAAGGGGGSG SLSLRGLKQR ETGKEVDAAD RV
//
