ID A0A2G5SSS1_9PELO Unreviewed; 435 AA.
AC A0A2G5SSS1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=MHD domain-containing protein {ECO:0000259|PROSITE:PS51072};
GN Name=Cni-dpy-23 {ECO:0000313|EMBL:PIC18080.1};
GN Synonyms=Cnig_chr_X.g24102 {ECO:0000313|EMBL:PIC18080.1};
GN ORFNames=B9Z55_024102 {ECO:0000313|EMBL:PIC18080.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC18080.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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 -!- 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:PIC18080.1}.
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DR EMBL; PDUG01000006; PIC18080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5SSS1; -.
DR Proteomes; UP000230233; Chromosome x.
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:UP000230233};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005992}.
FT DOMAIN 168..434
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 435 AA; 49722 MW; 8DF71D9DEF06EFBB CRC64;
MIGGLFVYNH KGEVLISRIY RDDVTRNAVD AFRVNVIHAR QQVRSPVTNM ARTSFFHVKR
GNVWICAVTR QNVNAAMVFE FLKRFADTMQ SYFGKLNEEN VKNNFVLIYE LLDEILDFGY
PQNTDPGVLK TFITQQGVRT ATKEEQSQIT SQVTGQIGWR REGIKYRRNE LFLDVIEYVN
LLMNQQGQVL SAHVAGKVAM KSYLSGMPEC KFGINDKITI EGKSKPGSDD PNKASRAAVA
IDDCQFHQCV KLTKFETEHA ISFIPPDGEY ELMRYRTTKD IQLPFRVIPL VREVSRNKME
VKVVVKSNFK PSLLAQKIEV RIPTPPNTSG VQLICMKGKA KYKAGENAIV WKIKRMAGMK
ESQISAEIDL LSTGNVEKKK WNRPPVSMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
WVRYIGRSGL YETRC
//
