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Database: UniProt
Entry: A0A1V9YFM4_9STRA
LinkDB: A0A1V9YFM4_9STRA
Original site: A0A1V9YFM4_9STRA 
ID   A0A1V9YFM4_9STRA        Unreviewed;      1261 AA.
AC   A0A1V9YFM4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Transmembrane protein {ECO:0000313|EMBL:OQR84545.1};
GN   ORFNames=ACHHYP_13259 {ECO:0000313|EMBL:OQR84545.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR84545.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR84545.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR84545.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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:OQR84545.1}.
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DR   EMBL; JNBR01001851; OQR84545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9YFM4; -.
DR   STRING; 1202772.A0A1V9YFM4; -.
DR   OrthoDB; 5479304at2759; -.
DR   Proteomes; UP000243579; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005227; F:calcium-activated cation channel activity; IEA:InterPro.
DR   InterPro; IPR045122; Csc1-like.
DR   InterPro; IPR027815; CSC1/OSCA1-like_cyt.
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.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:OQR84545.1};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        274..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..824
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        844..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        883..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        952..982
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1002..1026
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1090..1111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1117..1136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          459..609
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1235..1261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1236..1252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1261 AA;  138197 MW;  41E856EABCC0E515 CRC64;
     MTVVRLPPLP TPPVVHLAEA DVEVTSPPTI DQPSTEPSTN SLGTATGNSG TTAEPPTITA
     EPIALPATDL QSIDDKSPTV VQSFDDETPS AAHTIDDETP AELNASDVGS EAPQSAPNSP
     EECPSDATTV TAPADASCAD DNEWADEANA LQSSADLVPE AMLEKYENSD TEAAVWGPST
     NAVGFNSSAA CEANAAPPIT AANTPAVGEA VGQGATGRPG SAKKPLTRVA MISHAQALAA
     AERLGAGKSF FHTTMKDISE LGVGLQLYFM FTKYMGLCFL GMSVLALPAL IMHGSGYGID
     TQMIDPMRLS LYTMANEGVN STGNATTQWC LGNPFTQDPF TTSYIITACD LLYSAGFVFF
     IWYFKHASNQ VIAMQADAIT PAKYAVFVRG LPPSATEASV LQHFNQRYNP TADRKEFPMR
     MGCWGRPRPP KHRPDLTHGG RLTAPVSNTD HLVHGPNALY VGTFIAEVSI AHPTGGLLRT
     FLAMEHLTAK VAELNDILST LKSPAAEVPD RDKLTTKVEE QLEKVTDTLE RKTARMKELR
     ANGASTVEAC ECAFVVFNSV EAQQRCLRDY RTSGYSYARY FQPKDLRFEG KYPLHVRQAP
     EPSNIMWENL EVSATERRLR RYFTNFITFL LLLLSCAIIS LAQSAQAKFS AATIPNFCSE
     ALPAVFTGNY STIPNYAWKL YWNQYPNVTC PLGSYYVGYT NKVAVTVPAR GNATQCLGHC
     ISTTTTLDKT CSTLPCFDPA LVDLKTRPCT TYLASDLLKC YCEPALERAI QLYGWIDGPR
     KMYNYELPCQ GYLKNYLAKN SALFLAAVTV IVVNLFLQTV LRAFADFERH TSESDRTSAM
     VLKLFFAQLL NTGIIVLLVN ANLSNVPLPL SLSEILHGQF DDFVRQWYIS VGVGISTTMI
     INAVSPQLGP LLQTYVIGPI RRWRALRAAV TQKQMNELFA GPPFDISLRY PLVLNTVFVT
     MMYCGGIPIL LPVASLSCLV MHQLDKLTIM RLYSVRTAYD EALGQLSLAM LPLALLLHLA
     FSTWMYGNDH FLQSNLINVP WLLKTLGFNS NATGVDAVYA ELQAAVSQYD PLGKHGLSSK
     IWRVNDFPMF VFFIVALVSY LLTTFFGVLL WPLAEKPLLL LFKLLSLVCS SAAEALKRAL
     RRRTYSPTAA IVAQYPDFTG VFQVASTTKK VDSAKGFELQ ENGVLIRKWT VETDRRNAGD
     RMLTWEAMAA PVKTYSIYAN PKYRNAVNEL SNARERVGAE QPKLEAPRKK KPAKTSVVVP
     T
//
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