ID   AP2B_SCHPO              Reviewed;         677 AA.
AC   O43005;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=AP-2 complex subunit beta;
DE   AltName: Full=Beta-2-adaptin;
DE   AltName: Full=Beta-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 2 beta large chain;
DE   AltName: Full=Clathrin assembly protein large beta chain;
GN   Name=apl1; ORFNames=SPBC2G2.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Adaptins are components of the adaptor complexes which link
CC       clathrin to receptors in coated vesicles. Clathrin-associated protein
CC       complexes are believed to interact with the cytoplasmic tails of
CC       membrane proteins, leading to their selection and concentration. Beta
CC       adaptin is a subunit of the plasma membrane adaptor (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC       of two large adaptins (alpha-type subunit apl3 and beta-type subunit
CC       apl1), a medium chain (mu-type subunit apm4) and a small adaptin
CC       (sigma-type subunit aps2). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles in the plasma membrane.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA17886.1; -; Genomic_DNA.
DR   PIR; T40145; T40145.
DR   RefSeq; NP_596435.1; NM_001022354.2.
DR   AlphaFoldDB; O43005; -.
DR   SMR; O43005; -.
DR   BioGRID; 276904; 7.
DR   STRING; 4896.SPBC2G2.06c.1; -.
DR   iPTMnet; O43005; -.
DR   MaxQB; O43005; -.
DR   PaxDb; O43005; -.
DR   PRIDE; O43005; -.
DR   EnsemblFungi; SPBC2G2.06c.1; SPBC2G2.06c.1:pep; SPBC2G2.06c.
DR   GeneID; 2540375; -.
DR   KEGG; spo:SPBC2G2.06c; -.
DR   PomBase; SPBC2G2.06c; apl1.
DR   VEuPathDB; FungiDB:SPBC2G2.06c; -.
DR   eggNOG; KOG1061; Eukaryota.
DR   HOGENOM; CLU_006320_4_4_1; -.
DR   InParanoid; O43005; -.
DR   OMA; KMCFLYL; -.
DR   PhylomeDB; O43005; -.
DR   Reactome; R-SPO-437239; Recycling pathway of L1.
DR   Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-SPO-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-SPO-8964038; LDL clearance.
DR   PRO; PR:O43005; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030122; C:AP-2 adaptor complex; ISO:PomBase.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IC:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR026739; AP_beta.
DR   InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   PANTHER; PTHR11134; PTHR11134; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Coated pit; Endocytosis; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..677
FT                   /note="AP-2 complex subunit beta"
FT                   /id="PRO_0000193754"
FT   REGION          597..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  76535 MW;  F99EEE797EAD0266 CRC64;
     MSSSSSHFSS TAADLLAVFS SDNKDKSANK RISALKKAIA GISYGYDMSS LFPSVISSME
     SNNLELKKLC YLYLKIYASV KPTEAKRAVK LILNDIYSSN PMIRSLALRT LTSVNIKNFW
     VAAMDPIVRL LDDTDPYVRK TAAIGIAKLY SYDKKMVESS GLIDHLKEML SDESSVVVAN
     SLAALMNIVN SSTGFKLTFS REISNKLVKS LTDCSEWLQV AILDALIFYV PQKPGEAESF
     AERISPWLQH GNAAVCMGAV KVILYLTNYM KDDNRVKEYF MKTQPPLVTL LARKSSATQY
     VILRNIQIIL EQCPEMFAND IHFFYCNFDD PIYVKLEKLD ILTKIADIHN LDQILPEFVE
     YASEIDVELV RKSVKCIGYL AIKIEERKND CIDSLIELMN TKVTYVIQEA VIVIRDILRK
     YPGSYKSLVP ILYENLDSLD EPDAKSAVIW ILGQYAEEIE DSITLLNDYL KGFFDEPLEI
     QLTLLTAVIK VFLKKPTAAA DMVTNVLQWC TDEVNDPDLR DRGIIYSRML SANPELAKKV
     ILANMPPVNV GTGMYDPDTT EQLMLNISTL SSIYHKPPNR FVKGAQVAYC EPSPVLRLRT
     RDSNPSNTDS RESNHKKYNH FHQKSQTRRV MEQYDRNSWN PSPFSDESNS NTFSGKFDSA
     DQENLGMPMT PETHLMD