AP1M2_BOVIN
ID AP1M2_BOVIN Reviewed; 423 AA.
AC Q3SYW1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=AP-1 complex subunit mu-2;
DE AltName: Full=AP-mu chain family member mu1B;
DE AltName: Full=Adaptor protein complex AP-1 subunit mu-2;
DE AltName: Full=Adaptor-related protein complex 1 subunit mu-2;
DE AltName: Full=Clathrin assembly protein complex 1 mu-2 medium chain 2;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin mu-2 subunit;
DE AltName: Full=Mu-adaptin 2;
DE AltName: Full=Mu1B-adaptin;
GN Name=AP1M2 {ECO:0000250|UniProtKB:Q9Y6Q5};
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:AAI03359.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI03359.1};
RC TISSUE=Ileum {ECO:0000312|EMBL:AAI03359.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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:Q9Y6Q5,
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 P2X4 (By similarity). {ECO:0000250|UniProtKB:D3ZRP6}.
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}.
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DR EMBL; BC103358; AAI03359.1; -; mRNA.
DR RefSeq; NP_001029683.1; NM_001034511.1.
DR AlphaFoldDB; Q3SYW1; -.
DR SMR; Q3SYW1; -.
DR STRING; 9913.ENSBTAP00000043007; -.
DR PaxDb; Q3SYW1; -.
DR PeptideAtlas; Q3SYW1; -.
DR PRIDE; Q3SYW1; -.
DR Ensembl; ENSBTAT00000045632; ENSBTAP00000043007; ENSBTAG00000021160.
DR GeneID; 515766; -.
DR KEGG; bta:515766; -.
DR CTD; 10053; -.
DR VEuPathDB; HostDB:ENSBTAG00000021160; -.
DR VGNC; VGNC:25980; AP1M2.
DR eggNOG; KOG0937; Eukaryota.
DR GeneTree; ENSGT00940000159089; -.
DR HOGENOM; CLU_026996_0_0_1; -.
DR InParanoid; Q3SYW1; -.
DR OMA; FMWIKYS; -.
DR OrthoDB; 725236at2759; -.
DR TreeFam; TF300393; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000021160; Expressed in corpus epididymis and 77 other tissues.
DR ExpressionAtlas; Q3SYW1; 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; 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 Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..423
FT /note="AP-1 complex subunit mu-2"
FT /id="PRO_0000240591"
FT DOMAIN 168..421
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ SEQUENCE 423 AA; 48150 MW; D86D5545582E361F CRC64;
MSASAVFILD VKGKPLISRN YKGDVAMSEI DHFMPLLMQR EEEGALTPLL SHGRVHFLWI
KYSNLYLVAT TLKNANASLV YSFLYKIVEV FSEYFKELEE ESIRDNFVIV YELLDELMDF
GFPQTTDSKI LQEYITQQGN KLETGKSRVP PTVTNAVSWR SEGIKYKKNE VFIDVIESVN
LLVNANGSVL LSEIVGSIKL KVFLSGMPEL RLGLNDRVLF ELTGRSKNKS VELEDVKFHQ
CVRLSRFDND RTISFIPPDG DFELMSYRLS TQVKPLIWIE SVIEKFSHSR VEIMVKAKGQ
FKKQSVANGV EISVPVPSDA DSPRFKTSVG SAKYVPEKNT VIWSIKSFPG GKEYLMRAHF
GLPSVEKEEV EGRPPIGVKF EIPYFTVSGI QVRYMKIIEK SGYQALPWVR YITQSGDYQL
RTS
