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Database: UniProt
Entry: A0A2V0P6H3_9CHLO
LinkDB: A0A2V0P6H3_9CHLO
Original site: A0A2V0P6H3_9CHLO 
ID   A0A2V0P6H3_9CHLO        Unreviewed;       707 AA.
AC   A0A2V0P6H3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   RecName: Full=ENTH domain-containing protein {ECO:0000259|PROSITE:PS50942};
GN   ORFNames=Rsub_08420 {ECO:0000313|EMBL:GBF95458.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF95458.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF95458.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF95458.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       {ECO:0000256|ARBA:ARBA00004132}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}. Membrane, clathrin-coated pit
CC       {ECO:0000256|ARBA:ARBA00004600}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
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:GBF95458.1}.
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DR   EMBL; BDRX01000064; GBF95458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0P6H3; -.
DR   STRING; 307507.A0A2V0P6H3; -.
DR   InParanoid; A0A2V0P6H3; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR   CDD; cd03564; ANTH_N; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 1.20.58.150; ANTH domain; 1.
DR   InterPro; IPR011417; ANTH_dom.
DR   InterPro; IPR014712; ANTH_dom_sf.
DR   InterPro; IPR048050; ANTH_N_plant.
DR   InterPro; IPR045192; AP180-like.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   PANTHER; PTHR22951; CLATHRIN ASSEMBLY PROTEIN; 1.
DR   PANTHER; PTHR22951:SF5; PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN LAP; 1.
DR   Pfam; PF07651; ANTH; 2.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF89009; GAT-like domain; 1.
DR   PROSITE; PS50942; ENTH; 1.
PE   4: Predicted;
KW   Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT   DOMAIN          5..144
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   REGION          234..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..461
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  72510 MW;  E1243B685EFB27BC CRC64;
     MDALVLQQKA KDLYVAVTKA TLPDDKPPKE KHVRTLKIAC SAHAPRPQVD FVIYKLGKRL
     GSPHWVIAGK ALMVFHRLMR ECDPSFLEQL LRYCDRTGRP RLLCLDRYAD HSSREAWDYS
     AWVRAYGVYL DERLDAFRSM RFDPEAGNPA RHQLAAFGYG GALGGPTGGP TGGFGGPTGG
     YGGPTGGYGG PTGGYGGPTG GYGGPTGGYG GPTGGYGGPT GGYGGGYGGP PGGYGGPTGG
     AGFANGGQQI QQQHPGQQGG PQLGQQLTGQ SGQGQAQSGT SLKDCAASEL LDLLPRMQRL
     MLRVLACVPE GAAAYNPICL TGAAWVLRES KAVYRAASEG VINLADSFFD MGRADAMRGL
     ELYRDAIALH ERLTSYYSTM QAVPALRTAI NYPSLQPLPA DFLQTMEKYA REAPREGAPA
     KSKVEPAPAA EEAPAPEEDP QPPPQPEPEP EPAPAPQEPE PVVSPVKAAL APVIDLLSFD
     DGPSEAVAAA AEAAPGVLDD LADGLTAPQG AQQQQGGAAA QGQAGQQPQG QYGGYPPQYT
     GYGGYPPQYT GYGGYGGYGG YAPQFTGYGG YGGYAAPTSM ALVPVGPMGV NPFMPGGASA
     SQQLQPYGSL APFAAAAPAA TGAAPANPNN PFANGGAGGG GGNGGGGAFV GKRLEGDPLN
     ELTEQFLGPR PKPKTAEAVG ARASLKDLKA AARAVVADSA SSPRAAV
//
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