AP1M2_MOUSE
ID AP1M2_MOUSE Reviewed; 423 AA.
AC Q9WVP1; Q99LA4; Q9CWP7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 151.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=10338135; DOI=10.1016/s0014-5793(99)00432-9;
RA Ohno H., Tomemori T., Nakatsu F., Okazaki Y., Aguilar R.C., Foelsch H.,
RA Mellman I., Saito T., Shirasawa T., Bonifacino J.S.;
RT "Mu1B, a novel adaptor medium chain expressed in polarized epithelial
RT cells.";
RL FEBS Lett. 449:215-220(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10640811; DOI=10.1159/000015391;
RA Nakatsu F., Kadohira T., Gilbert D.J., Jenkins N.A., Kakuta H.,
RA Copeland N.G., Saito T., Ohno H.;
RT "Genomic structure and chromosome mapping of the genes encoding clathrin-
RT associated adaptor medium chains mu1A (Ap1m1) and mu1B (Ap1m2).";
RL Cytogenet. Cell Genet. 87:53-58(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [5]
RP IDENTIFICATION IN THE AP-1 COMPLEX.
RX PubMed=11964383; DOI=10.1093/embo-reports/kvf092;
RA Eskelinen E.L., Meyer C., Ohno H., von Figura K., Schu P.;
RT "The polarized epithelia-specific mu 1B-adaptin complements mu 1A-
RT deficiency in fibroblasts.";
RL EMBO Rep. 3:471-477(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
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 ECO:0000269|PubMed:11964383}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WVP1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVP1-2; Sequence=VSP_000170;
CC -!- PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its
CC affinity for sorting signals. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AF067146; AAD28085.1; -; mRNA.
DR EMBL; AF139416; AAF61815.1; -; Genomic_DNA.
DR EMBL; AF139406; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139407; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139408; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139409; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139410; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139411; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139412; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139413; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139414; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AF139415; AAF61815.1; JOINED; Genomic_DNA.
DR EMBL; AK010478; BAB26971.1; -; mRNA.
DR EMBL; BC003704; AAH03704.1; -; mRNA.
DR CCDS; CCDS22902.1; -. [Q9WVP1-1]
DR CCDS; CCDS52734.1; -. [Q9WVP1-2]
DR RefSeq; NP_001103770.1; NM_001110300.1.
DR RefSeq; NP_033808.2; NM_009678.2.
DR AlphaFoldDB; Q9WVP1; -.
DR SMR; Q9WVP1; -.
DR ComplexPortal; CPX-5144; Endothelial AP-1 Adaptor complex, sigma1a variant.
DR STRING; 10090.ENSMUSP00000111093; -.
DR iPTMnet; Q9WVP1; -.
DR PhosphoSitePlus; Q9WVP1; -.
DR jPOST; Q9WVP1; -.
DR MaxQB; Q9WVP1; -.
DR PaxDb; Q9WVP1; -.
DR PeptideAtlas; Q9WVP1; -.
DR PRIDE; Q9WVP1; -.
DR ProteomicsDB; 296323; -. [Q9WVP1-1]
DR ProteomicsDB; 296324; -. [Q9WVP1-2]
DR DNASU; 11768; -.
DR GeneID; 11768; -.
DR KEGG; mmu:11768; -.
DR UCSC; uc009okx.2; mouse. [Q9WVP1-1]
DR UCSC; uc009oky.2; mouse. [Q9WVP1-2]
DR CTD; 10053; -.
DR MGI; MGI:1336974; Ap1m2.
DR eggNOG; KOG0937; Eukaryota.
DR InParanoid; Q9WVP1; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; Q9WVP1; -.
DR TreeFam; TF300393; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 11768; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ap1m2; mouse.
DR PRO; PR:Q9WVP1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WVP1; protein.
DR GO; GO:0030121; C:AP-1 adaptor complex; IC:ComplexPortal.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; IC:ComplexPortal.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0110010; P:basolateral protein secretion; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
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 Alternative splicing; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..423
FT /note="AP-1 complex subunit mu-2"
FT /id="PRO_0000193773"
FT DOMAIN 168..421
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT VAR_SEQ 225
FT /note="R -> LSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000170"
FT CONFLICT 112
FT /note="D -> E (in Ref. 3; BAB26971 and 4; AAH03704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48137 MW; FD18049309F074B5 CRC64;
MSASAVFILD VKGKPLISRN YKGDVPMTEI DHFMPLLMQR EEEGVLAPLL SHGRVHFLWI
KHSNLYLVAT TLKNANASLV YSFLYKTVEV FCEYFKELEE ESIRDNFVIV YDLLDELMDF
GFPQTTDSKI LQEYITQQGN KLETGKSRVP PTVTNAVSWR SEGIKYKKNE VFIDVIESVN
LLVNANGSVL LSEIVGTIKL KVFLSGMPEL RLGLNDRVLF ELTGRSKNKS VELEDVKFHQ
CVRLSRFDND RTISFIPPDG DFELMSYRLS TQVKPLIWIE SVIEKFSHSR VEIMVKAKGQ
FKKQSVANGV EISVPVPSDA DSPRFKTSVG SAKYVPEKNV VIWSIKSFPG GKEYLMRAHF
GLPSVETEEV EGRPPIGVKF EIPYFTVSGI QVRYMKIIEK SGYQALPWVR YITQSGDYQL
RTS
