ID A0A093VSF3_TALMA Unreviewed; 1068 AA.
AC A0A093VSF3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Endocytosis protein end4 {ECO:0000313|EMBL:KFX49556.1};
GN ORFNames=GQ26_0091730 {ECO:0000313|EMBL:KFX49556.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX49556.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX49556.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX49556.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
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:KFX49556.1}.
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DR EMBL; JPOX01000009; KFX49556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VSF3; -.
DR eggNOG; KOG0980; Eukaryota.
DR HOGENOM; CLU_004601_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR10407:SF15; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR Pfam; PF07651; ANTH; 3.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF109885; I/LWEQ domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 1..156
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 825..1068
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 304..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1027..1054
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 308..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 121012 MW; FB8578D96658EE40 CRC64;
MSRTEADLAV NIRKATSIEE TAPKSTIKPP SLLPPRVDAA SAPVRSRSLI WRGLRLNIAR
QPILADEVQT FKALITIHKV LQEGHPIAIR EAQTHVNWLD SLMRGVAGEG LRGLFEYEEY
ISLKTINDPN EGYEAIMDLM NLQDQIDSFQ KLIFSHFQNG TNNECRISAL VPLVQESYGI
YKFITSMLRA MHSLATFPPS FAGRHTGPAL QILYASNTYV VYDSSSTEFS SLIGIITDLM
CEDMLALVSF WFNGDLREST GDDEALEPLR SRYDAQHHRL VRFYYECSNL RYLTSLITVP
KLPQDPPSLL SEDDEQRPAL PKRPTNEVER EPSPPPKAAA PEPEPINDFW NAEARRQQEE
FEAEQRRLQQ QWEDQQRQQM QAQQQAQRDF EEQQRLQAEQ QRLAQEALLR DQYAQHTQGR
MAELEQENLN ARAQYERDQL LLQQYDKRMK DLEEQLNNLN GNFNLQMNSK DDQIKALQEQ
VNTWRSKYEA LAKLYSQLRQ EHLDLLQTTK ALKLKAASAQ EAIDKREKLE REMKTKNLEL
ADMIRERDRA LHDRDRLTGT NKEELEKLKR ELRLAIERAE NAERQKGSEI SSMLSKYNRE
MADLEEALRN KTRALEEYTS KRGELSEDHE LALREKDEEI EVYKSGMEQA LMELEELKLS
QGDVDHALDS QIDEVLHGTV AKINDIIDSV LQSGVQRVDD ALYELESSNQ AGNQSATPAY
VLSQVEKASA SATDFNIPGS IADVLSNTKG LTRFATDDKN SDQLINAARK PAQATIRFLR
GLQSFRLEGL EPLQKTDVVI NNNLEVQRDL QTLSKFVDTF APKGSKISTS GDLGNLVDQE
LEKAANAIDA AVERLARLRK KPRDGFTTYE LRVNDTILEA ALAITNAIAE LIKAATESQQ
EIVREGRGSS SRTAFYKKNN RWTEGLISAA KAVATSTNRL IETADGVISG RNSPEQLIVA
SNDVAASTAQ LVAASRVKAT FMSRTQERLE TASKAVGAAC RSLVRQVQAI IAEKNKDEGE
SVDYSKLSGH EFKVREMEQQ VEILQLENAL SRARTRLGEM RKISYQEE
//
