AP1M1_BOVIN
ID AP1M1_BOVIN Reviewed; 423 AA.
AC Q2KJ81;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=AP-1 complex subunit mu-1;
DE AltName: Full=AP-mu chain family member mu1A;
DE AltName: Full=Adaptor protein complex AP-1 subunit mu-1;
DE AltName: Full=Adaptor-related protein complex 1 subunit mu-1;
DE AltName: Full=Clathrin assembly protein complex 1 mu-1 medium chain 1;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin mu-1 subunit;
DE AltName: Full=Mu-adaptin 1;
DE AltName: Full=Mu1A-adaptin;
GN Name=AP1M1 {ECO:0000250|UniProtKB:Q9BXS5};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI05478.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI05478.1};
RC TISSUE=Hypothalamus {ECO:0000312|EMBL:AAI05478.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=12604586; DOI=10.1083/jcb.200211080;
RA Ghosh P., Kornfeld S.;
RT "AP-1 binding to sorting signals and release from clathrin-coated vesicles
RT is regulated by phosphorylation.";
RL J. Cell Biol. 160:699-708(2003).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the trans-Golgi network (TGN) and
CC endosomes. The AP complexes mediate the recruitment of clathrin to
CC membranes and the recognition of sorting signals within the cytosolic
CC tails of transmembrane cargo molecules. {ECO:0000250|UniProtKB:Q9BXS5,
CC ECO:0000269|PubMed:12604586}.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Interacts with
CC MARCHF11 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex. {ECO:0000250}.
CC -!- PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its
CC affinity for sorting signals. {ECO:0000269|PubMed:12604586}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI05478.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC105477; AAI05478.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001039349.2; NM_001045884.2.
DR AlphaFoldDB; Q2KJ81; -.
DR SMR; Q2KJ81; -.
DR STRING; 9913.ENSBTAP00000017724; -.
DR PaxDb; Q2KJ81; -.
DR PRIDE; Q2KJ81; -.
DR Ensembl; ENSBTAT00000017724; ENSBTAP00000017724; ENSBTAG00000013329.
DR GeneID; 504310; -.
DR KEGG; bta:504310; -.
DR CTD; 8907; -.
DR VEuPathDB; HostDB:ENSBTAG00000013329; -.
DR VGNC; VGNC:25979; AP1M1.
DR eggNOG; KOG0937; Eukaryota.
DR GeneTree; ENSGT00940000157924; -.
DR HOGENOM; CLU_026996_0_2_1; -.
DR InParanoid; Q2KJ81; -.
DR OMA; CRAKAQI; -.
DR OrthoDB; 725236at2759; -.
DR TreeFam; TF300393; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000013329; Expressed in spermatid and 104 other tissues.
DR ExpressionAtlas; Q2KJ81; baseline and differential.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0035615; F:clathrin adaptor activity; 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; 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 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 Acetylation; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS5"
FT CHAIN 2..423
FT /note="AP-1 complex subunit mu-1"
FT /id="PRO_0000240589"
FT DOMAIN 168..421
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS5"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS5"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS5"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q32Q06"
SQ SEQUENCE 423 AA; 48587 MW; 64EC5E47EA6F8E98 CRC64;
MSASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL AHGGVRFMWI
KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF
GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR SEGIKYRKNE VFLDVIESVN
LLVSANGNVL RSEIVGSIKM RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ
CVRLSRFEND RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMIKAKSQ
FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSIKSFPG GKEYLMRAHF
GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK SGYQALPWVR YITQNGDYQL
RTQ
