ID F1RD00_DANRE Unreviewed; 436 AA.
AC F1RD00; A0A8M2B673;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=AP-2 complex subunit mu-B {ECO:0000313|Ensembl:ENSDARP00000100738, ECO:0000313|RefSeq:XP_005159313.1};
GN Name=ap2m1b {ECO:0000313|Ensembl:ENSDARP00000100738,
GN ECO:0000313|RefSeq:XP_005159313.1,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-1103};
GN Synonyms=ap2m1 {ECO:0000313|RefSeq:XP_005159313.1}, zgc:56643
GN {ECO:0000313|RefSeq:XP_005159313.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000100738};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000100738}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000100738};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000126276}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000126276};
RG Ensembl;
RL Submitted (MAY-2012) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000100738, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000100738};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:XP_005159313.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005159313.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00005324, ECO:0000256|PIRNR:PIRNR005992}.
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DR EMBL; CU855919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005159313.1; XM_005159256.4.
DR Ensembl; ENSDART00000108636.4; ENSDARP00000100738.3; ENSDARG00000033899.8.
DR Ensembl; ENSDART00000151418.3; ENSDARP00000126276.1; ENSDARG00000033899.8.
DR GeneID; 394001; -.
DR AGR; ZFIN:ZDB-GENE-040426-1103; -.
DR CTD; 394001; -.
DR ZFIN; ZDB-GENE-040426-1103; ap2m1b.
DR OMA; MPICELS; -.
DR OrthoDB; 6959at2759; -.
DR TreeFam; TF300722; -.
DR Proteomes; UP000000437; Chromosome 18.
DR Bgee; ENSDARG00000033899; Expressed in intestine and 26 other cell types or tissues.
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:UP000000437};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005992}.
FT DOMAIN 170..435
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT BINDING 342
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 344
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 346
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 355
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 357
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 436 AA; 49739 MW; 1A00774844F6B04D CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMT AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QHHTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIDKQGKGGT TDDTGKSGKQ
SIAIDDCTFH QCVRLSKFDS ERSISFIPPD GEYELMRYRT TKDIILPFRV IPLVREVGRT
KLEVKVVIKS NFKPSLLAQK IEVRIPTPLN TSGVQVICMK GKAKYKASEN AIVWKIKRMA
GMKESQISAE IELLPTNDKK KWARPPISMN FEVPFAPSGL KVRYLKVFEP KLNYSDHDVI
KWVRYIGRSG IYETRC
//
