AP3M1_RAT
ID AP3M1_RAT Reviewed; 418 AA.
AC P53676;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=AP-3 complex subunit mu-1;
DE AltName: Full=AP-3 adaptor complex mu3A subunit;
DE AltName: Full=Adaptor-related protein complex 3 subunit mu-1;
DE AltName: Full=Clathrin assembly protein assembly protein complex 3 mu-1 medium chain;
DE AltName: Full=Clathrin coat assembly protein AP47 homolog 1;
DE AltName: Full=Clathrin coat-associated protein AP47 homolog 1;
DE AltName: Full=Golgi adaptor AP-1 47 kDa protein homolog 1;
DE AltName: Full=HA1 47 kDa subunit homolog 1;
DE AltName: Full=Mu-adaptin 3A;
DE AltName: Full=Mu3A-adaptin;
DE AltName: Full=P47A;
GN Name=Ap3m1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
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: Part of the AP-3 complex, an adaptor-related complex which is
CC not clathrin-associated. The complex is associated with the Golgi
CC region as well as more peripheral structures. It facilitates the
CC budding of vesicles from the Golgi membrane and may be directly
CC involved in trafficking to lysosomes. In concert with the BLOC-1
CC complex, AP-3 is required to target cargos into vesicles assembled at
CC cell bodies for delivery into neurites and nerve terminals (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of two large adaptins (delta-type subunit AP3D1 and beta-type subunit
CC AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and
CC a small adaptin (sigma-type subunit APS1 or AP3S2). Interacts with
CC AGAP1. AP-3 associates with the BLOC-1 complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Component of the coat surrounding the
CC cytoplasmic face of coated vesicles located at the Golgi complex.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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; L07073; AAA57231.1; -; mRNA.
DR PIR; I84763; I84763.
DR PDB; 4IKN; X-ray; 1.85 A; A=165-418.
DR PDBsum; 4IKN; -.
DR AlphaFoldDB; P53676; -.
DR SMR; P53676; -.
DR IntAct; P53676; 10.
DR MINT; P53676; -.
DR STRING; 10116.ENSRNOP00000016387; -.
DR jPOST; P53676; -.
DR PaxDb; P53676; -.
DR PRIDE; P53676; -.
DR UCSC; RGD:620417; rat.
DR RGD; 620417; Ap3m1.
DR eggNOG; KOG2740; Eukaryota.
DR InParanoid; P53676; -.
DR PhylomeDB; P53676; -.
DR PRO; PR:P53676; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..418
FT /note="AP-3 complex subunit mu-1"
FT /id="PRO_0000193783"
FT DOMAIN 176..417
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT STRAND 178..191
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 197..211
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:4IKN"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:4IKN"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 288..300
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 318..332
FT /evidence="ECO:0007829|PDB:4IKN"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:4IKN"
FT STRAND 402..416
FT /evidence="ECO:0007829|PDB:4IKN"
SQ SEQUENCE 418 AA; 46981 MW; 3DFA24B1B954B5BF CRC64;
MIHSLFLINC SGDIFLEKHW KSVVSQSVCD YFFEAQEKAA DVENVPTVIS TPHHYLISIY
RDKLFFVSVI QTEVPPLFVI EFLHRVADTF QDYFGECSEA AIKDNVVIVY ELLEEMLDNG
FPLATESNIL KELIKPPTIL RSVVNSITGS SNVGDTLPTG QLSNIPWRRA GVKYTNNEAY
FDVVEEIDAI IDKSGSTVFA EIQGVIDACI KLSGMPDLSL SFMNPRLLDD VSFHPCIRFK
RWESERVLSF IPPDGNFRLI SYRVSSQNLV AIPVYVKHNI SFKENSSCGR FDITIGPKQN
MGKTIEGITV TVHMPKVVLN MNLTPTQGSY TFDPVTKVLA WDVGKITPQK LPSLKGLVNL
QSGAPKPEEN PNLNIQFKIQ QLAISGLKVN RLDMYGEKYK PFKGVKYITK AGKFQVRT
