ID   AP1M2_RAT               Reviewed;         423 AA.
AC   D3ZRP6;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 2.
DT   03-AUG-2022, entry version 72.
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   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 GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   INTERACTION WITH P2X4.
RX   PubMed=15985462; DOI=10.1242/jcs.02451;
RA   Royle S.J., Qureshi O.S., Bobanovic L.K., Evans P.R., Owen D.J.,
RA   Murrell-Lagnado R.D.;
RT   "Non-canonical YXXGPhi endocytic motifs: recognition by AP2 and
RT   preferential utilization in P2X4 receptors.";
RL   J. Cell Sci. 118:3073-3080(2005).
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   -!- 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 P2X4 (PubMed:15985462). {ECO:0000250|UniProtKB:Q9Y6Q5,
CC       ECO:0000269|PubMed:15985462}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q9Y6Q5}.
CC       Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC       {ECO:0000250|UniProtKB:Q9Y6Q5}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9Y6Q5}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9Y6Q5}. Note=Component of the coat surrounding
CC       the cytoplasmic face of coated vesicles located at the Golgi complex.
CC       {ECO:0000250|UniProtKB:Q9Y6Q5}.
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; AABR07069448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07073371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 10116.ENSRNOP00000063098; -.
DR   PhosphoSitePlus; D3ZRP6; -.
DR   jPOST; D3ZRP6; -.
DR   PaxDb; D3ZRP6; -.
DR   PeptideAtlas; D3ZRP6; -.
DR   PRIDE; D3ZRP6; -.
DR   UCSC; RGD:1561490; rat.
DR   RGD; 1561490; Ap1m2.
DR   VEuPathDB; HostDB:ENSRNOG00000043093; -.
DR   eggNOG; KOG0937; Eukaryota.
DR   HOGENOM; CLU_026996_0_0_1; -.
DR   InParanoid; D3ZRP6; -.
DR   OMA; FMWIKYS; -.
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   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000043093; Expressed in duodenum and 13 other tissues.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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_0000455631"
FT   DOMAIN          168..421
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ   SEQUENCE   423 AA;  48167 MW;  42DF9783A7262F0A CRC64;
     MSASAVFILD VKGKPLISRN YKGDVPMTEI DHFMPLLMQR EEEGMLAPLL SHGRVHFLWI
     KHSNLYLVAT TLKNANASLV YSFLYKTVEV FCEYFKELEE ESIRDNFVIV YELLDELMDF
     GFPQTTDSKI LQEYITQQGN KLETGKSRVP PTVTNAVSWR SEGIKYKKNE VFIDVIESVN
     LLVNANGSVL LSEIVGTIKL KVFLSGMPEL RLGLNDRVLF ELTGRSKNKS VELEDVKFHQ
     CVRLSRFDND RTISFIPPDG DFELMSYRLS TQVRPRVDXE SVIEKFSHSR VEIMVKAKGQ
     FKKQSVANGV EISVPVPSDA DSPRFKTSVG SAKYVPEKNV VIWSIKSFPG GKEYLMRAHF
     GLPSVETEEV EGRPPIGVKF EIPYFTVSGI QVRYMKIIEK SGYQALPWVR YITQSGDYQL
     RTS