AP1M_DIPOM
ID AP1M_DIPOM Reviewed; 418 AA.
AC P47795;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=AP-1 complex subunit mu;
DE AltName: Full=Clathrin assembly protein complex 1 mu medium chain homolog;
DE AltName: Full=Clathrin coat assembly protein AP47 homolog;
DE AltName: Full=Clathrin coat-associated protein AP47 homolog;
DE AltName: Full=Golgi adaptor AP-1 47 kDa protein homolog;
DE AltName: Full=HA1 47 kDa subunit homolog;
DE AltName: Full=Mu-adaptin;
OS Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX NCBI_TaxID=1870830;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electric lobe;
RX PubMed=8076832; DOI=10.1016/0378-1119(94)90306-9;
RA Pevsner J., Volknandt W., Wong B.R., Scheller R.H.;
RT "Two rat homologs of clathrin-associated adaptor proteins.";
RL Gene 146:279-283(1994).
CC -!- FUNCTION: Component of the adapter complexes which link clathrin to
CC receptors in coated vesicles. Clathrin-associated protein complexes are
CC believed to interact with the cytoplasmic tails of membrane proteins,
CC leading to their selection and concentration. AP47 is a subunit of the
CC plasma membrane adapter.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma- and beta'-type subunits), a medium
CC adaptin (mu-type subunit AP47) and a small adaptin (sigma-type subunit
CC AP19).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex.
CC -!- PTM: Regulated by phosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; L07072; AAA57230.1; -; mRNA.
DR PIR; I50530; I50530.
DR AlphaFoldDB; P47795; -.
DR SMR; P47795; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR036168; AP2_Mu_C_sf.
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 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; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Transport.
FT CHAIN 1..418
FT /note="AP-1 complex subunit mu"
FT /id="PRO_0000193790"
FT DOMAIN 176..417
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ SEQUENCE 418 AA; 46772 MW; 3F25D57B7629979B CRC64;
MIHSLFLMNG GGAVFLEKHW RSVVSRSVCA YLLEAQLKAG QPENVAPVLA TPHHYLVSTH
RHGISFVAVI QAEVPPLFVI EFLHRVAETL QDYFGECSEA SIKDNVVIVY ELLEEMLDNG
FPLATESNIL KELIKPPTIL RSVVNSITGS SNVGDQLPTG QLSNIPWRRV GVKYTNNEAY
FDVTEEIDAI IDKSGSTVFA EIQGVIDACI KLTGMPDLTL SFLNPRLLDD VSFHPCVRFK
RWESERVLSF IPPVGNFRLM SYHVNSQNLV AIPVYVKHNI NFRDDGSTGW FDITIGPKQT
MGKVVENILV IIHMPKVVLN MTLTAAQGNF TFDPVTKVLI WDIGKIILPK LPTLKGLINL
QSGEAKPEEN PTLNIQFRIQ QLAVSGLKVN RLDMYGERYK PFKGVKYVTK AGKFQVRT