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Database: UniProt
Entry: A0A1B8GCU3_9PEZI
LinkDB: A0A1B8GCU3_9PEZI
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ID   A0A1B8GCU3_9PEZI        Unreviewed;       403 AA.
AC   A0A1B8GCU3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Endocytosis protein 3 {ECO:0000256|ARBA:ARBA00029684};
GN   Name=END3 {ECO:0000313|EMBL:OBT93659.1};
GN   ORFNames=VE01_08048 {ECO:0000313|EMBL:OBT93659.1};
OS   Pseudogymnoascus verrucosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT93659.1, ECO:0000313|Proteomes:UP000091956};
RN   [1] {ECO:0000313|EMBL:OBT93659.1, ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT93659.1,
RC   ECO:0000313|Proteomes:UP000091956};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
CC   -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC       required for the internalization of endosomes during actin-coupled
CC       endocytosis. The complex links the site of endocytosis to the cell
CC       membrane-associated actin cytoskeleton. Mediates uptake of external
CC       molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC       role in the proper organization of the cell membrane-associated actin
CC       cytoskeleton and promotes its destabilization.
CC       {ECO:0000256|ARBA:ARBA00025194}.
CC   -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC       {ECO:0000256|ARBA:ARBA00011159}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC       cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC       membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the END3 family.
CC       {ECO:0000256|ARBA:ARBA00009909}.
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DR   EMBL; KV460251; OBT93659.1; -; Genomic_DNA.
DR   RefSeq; XP_018127392.1; XM_018277476.1.
DR   AlphaFoldDB; A0A1B8GCU3; -.
DR   STRING; 342668.A0A1B8GCU3; -.
DR   GeneID; 28841434; -.
DR   OrthoDB; 12127at2759; -.
DR   Proteomes; UP000091956; Unassembled WGS sequence.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00052; EH; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000261; EH_dom.
DR   InterPro; IPR025604; End3.
DR   PANTHER; PTHR11216:SF74; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN END3; 1.
DR   PANTHER; PTHR11216; EH DOMAIN; 1.
DR   Pfam; PF12763; EF-hand_4; 1.
DR   Pfam; PF12761; End3; 1.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM00027; EH; 2.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 2.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091956}.
FT   DOMAIN          9..99
FT                   /note="EH"
FT                   /evidence="ECO:0000259|PROSITE:PS50031"
FT   DOMAIN          41..76
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          138..226
FT                   /note="EH"
FT                   /evidence="ECO:0000259|PROSITE:PS50031"
FT   REGION          234..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          294..351
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        234..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  45264 MW;  74E51327648D2333 CRC64;
     MAKRIEQQEI EKYWEIFASL SHGGTHLTGS QAAPVLKNSQ LNDDKLERIW DLADVDNDGS
     LDFEEFCVAM RLIFDIVNGE YADVPASLPD WLVPESKAHL VQASRALTGR QVQFEKVEDE
     DETLGLKDGF DWYMSPSDKS KYEEIYNANR DGRGEISFDT LEPLYSSLDV PDTDVKSAWN
     LINPNANSTI SKDATLAFLH ILNNRHEGFR IPRNVPPSLR ASFERNQIDY QVDNQRAGSP
     AQKWGSAGGE ETSTGRKAKF GDTYLSRLGV GGKSSYRPAG TDFSTTKTTE DWEEVRLKKQ
     LAELEAKVDK VEAASAKRHG GKRDTKPALV KRELEQLLDY KRRELREMET GEGKTKEGAG
     LKGVREEIEA VKEQVDGLGA HLRSRQSALE DLRQQVEDEK AGR
//
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