ID A0A158PJ86_ANGCS Unreviewed; 434 AA.
AC A0A158PJ86;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=MHD domain-containing protein {ECO:0000313|WBParaSite:ACOC_0000846101-mRNA-1};
GN ORFNames=ACOC_LOCUS8462 {ECO:0000313|EMBL:VDM60047.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000846101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000846101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM60047.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM60047.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral
CC membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004277}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000256|PIRNR:PIRNR005992}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYYA01004160; VDM60047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PJ86; -.
DR STRING; 334426.A0A158PJ86; -.
DR WBParaSite; ACOC_0000846101-mRNA-1; ACOC_0000846101-mRNA-1; ACOC_0000846101.
DR OMA; VWKIPRI; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR CDD; cd09251; AP-2_Mu2_Cterm; 1.
DR CDD; cd14836; AP2_Mu_N; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR043532; AP2_Mu_N.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR043512; Mu2_C.
DR PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 1.
DR PANTHER; PTHR10529:SF236; AP-2 COMPLEX SUBUNIT MU; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Lipid-binding {ECO:0000256|PIRSR:PIRSR005992-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR005992};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005992}.
FT DOMAIN 168..433
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT BINDING 339
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 341
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 343
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 352
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 354
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
SQ SEQUENCE 434 AA; 49486 MW; 36121D29CB1138D1 CRC64;
MIGGLFVYNH KGEVLISRIY RDDVTRNAVD AFRVNVIHAR QQVRTPVTNM ARTSFFHVKR
GNVWICAVTR QNVNAAMVFE FLNRFADTMQ SYFGKLNEEN VKNNFVLIYE LLDEILDFGY
PQNTDPGVLK TFITQQGVRT ATKEEQSQIT SQVTGQIGWR REGIKYRRNE LFLDVIEYVN
LLMSQQGQVL SAHVAGKVAM KSYLSGMPEC KFGINDKITI DGKGKTGGDD PNKSARASVA
IDDCQFHQCV KLTKFDTEHA ISFIPPDGEY ELMRYRTTKD IQLPFRVIPL VREVSRNKME
VKVVVKSNFK PSLLAQKIEV RIPTPPNTSG VQLICMKGKA KYKAGENAIV WKIKRMGGMK
ESQISAEIDL LSTGSEKKKW NRPPVSMNFE VPFAPSGLKV RYLKVFEPKL NYSDHDVIKW
VRYIGRSGLY ETRC
//
