AP1M1_RAT
ID AP1M1_RAT Reviewed; 423 AA.
AC Q32Q06;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
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:0000312|RGD:1307653};
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP INTERACTION WITH MARCHF11.
RX PubMed=17604280; DOI=10.1074/jbc.m700414200;
RA Morokuma Y., Nakamura N., Kato A., Notoya M., Yamamoto Y., Sakai Y.,
RA Fukuda H., Yamashina S., Hirata Y., Hirose S.;
RT "MARCH-XI, a novel transmembrane ubiquitin ligase implicated in ubiquitin-
RT dependent protein sorting in developing spermatids.";
RL J. Biol. Chem. 282:24806-24815(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXS5}.
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) (By similarity).
CC Interacts with MARCHF11. {ECO:0000250, ECO:0000269|PubMed:17604280}.
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:0000250|UniProtKB:Q2KJ81}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000255}.
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DR EMBL; BC107903; AAI07904.1; -; mRNA.
DR RefSeq; NP_001037704.1; NM_001044239.1.
DR AlphaFoldDB; Q32Q06; -.
DR SMR; Q32Q06; -.
DR BioGRID; 258420; 2.
DR IntAct; Q32Q06; 2.
DR MINT; Q32Q06; -.
DR STRING; 10116.ENSRNOP00000019350; -.
DR iPTMnet; Q32Q06; -.
DR PhosphoSitePlus; Q32Q06; -.
DR jPOST; Q32Q06; -.
DR PaxDb; Q32Q06; -.
DR PRIDE; Q32Q06; -.
DR GeneID; 306332; -.
DR KEGG; rno:306332; -.
DR UCSC; RGD:1307653; rat.
DR CTD; 8907; -.
DR RGD; 1307653; Ap1m1.
DR VEuPathDB; HostDB:ENSRNOG00000014454; -.
DR eggNOG; KOG0937; Eukaryota.
DR HOGENOM; CLU_026996_0_2_1; -.
DR InParanoid; Q32Q06; -.
DR OMA; CRAKAQI; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; Q32Q06; -.
DR TreeFam; TF300393; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q32Q06; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000014454; Expressed in testis and 19 other tissues.
DR Genevisible; Q32Q06; RN.
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:0035646; P:endosome to melanosome transport; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032438; P:melanosome organization; ISO:RGD.
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_0000240590"
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:0007744|PubMed:22673903"
SQ SEQUENCE 423 AA; 48557 MW; FED52CD7EA6803F7 CRC64;
MSASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL AHGGVRFMWI
KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF
GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR SEGIKYRKNE VFLDVIEAVN
LLVSANGNVL RSEIVGSIKM RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ
CVRLSRFEND RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMVKAKSQ
FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSIKSFPG GKEYLMRAHF
GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK SGYQALPWVR YITQNGDYQL
RTQ
