ID   AP1B1_SCHPO             Reviewed;         683 AA.
AC   O43079;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=AP-1 complex subunit beta-1;
DE   AltName: Full=Beta(1)-adaptin;
DE            Short=Beta-1-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 1 beta-1 large chain;
DE   AltName: Full=Clathrin assembly protein large beta-1 chain;
GN   Name=apl2; ORFNames=SPBC947.02;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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. The
CC       AP-1 complex interacts directly with clathrin (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC       of two large adaptins (gamma-type subunit apl4 and beta-type subunit
CC       apl2), a medium adaptin (mu-type subunit apm1) and a small adaptin
CC       (sigma-type subunit aps1). AP-1 interacts with clathrin (By
CC       similarity). {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; CAA17030.1; -; Genomic_DNA.
DR   PIR; T40780; T40780.
DR   RefSeq; NP_595274.1; NM_001021181.2.
DR   AlphaFoldDB; O43079; -.
DR   SMR; O43079; -.
DR   BioGRID; 277769; 9.
DR   STRING; 4896.SPBC947.02.1; -.
DR   iPTMnet; O43079; -.
DR   MaxQB; O43079; -.
DR   PaxDb; O43079; -.
DR   PRIDE; O43079; -.
DR   EnsemblFungi; SPBC947.02.1; SPBC947.02.1:pep; SPBC947.02.
DR   GeneID; 2541255; -.
DR   KEGG; spo:SPBC947.02; -.
DR   PomBase; SPBC947.02; apl2.
DR   VEuPathDB; FungiDB:SPBC947.02; -.
DR   eggNOG; KOG1061; Eukaryota.
DR   HOGENOM; CLU_006320_4_0_1; -.
DR   InParanoid; O43079; -.
DR   OMA; NPPEVQW; -.
DR   PhylomeDB; O43079; -.
DR   Reactome; R-SPO-432720; Lysosome Vesicle Biogenesis.
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:O43079; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030121; C:AP-1 adaptor complex; IDA:PomBase.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005768; C:endosome; IDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0099638; P:endosome to plasma membrane protein transport; IDA:PomBase.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA: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   1: Evidence at protein level;
KW   Cell membrane; Coated pit; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..683
FT                   /note="AP-1 complex subunit beta-1"
FT                   /id="PRO_0000193752"
FT   REGION          629..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   683 AA;  76682 MW;  6CE941C81E0EF422 CRC64;
     MVPKLFQSSR FKAFKKSETS ELQKGLVSQY AYERIDAVKR TIAAMTVGKD VSSLFPDVLK
     NLATRDITLK KLVYLYLINY AKTHPDLCIL AVNTFVKDSE EYNPTLRALA IRTMGCIRVN
     KIIGYLADPL RKALKDEHPY VRKAAAVCVV KMYDLDREYC ASNGFIEQLQ ALVSDPNPVV
     VANAVRSLAE IHDQDPEKGY FNVVYTMTDR LMVALSECNE WGRITILNSL ARFRTSDIKE
     AEYVCERVVP QFQHANSGVV LSAVKVIMVH IPLFSSDFTD FLYKKMAPPL LTLLSTDSEI
     QYVALRNINL ILQKRPSIFD VKTRVFFCKY NDPLYIKMEK LKIITMLACD ENINETISEL
     RAYVSEVELE FVKQTIKCLG DVALKVPSVI NDCISIFLEI YELNISYMVQ EVTVVMETVL
     RKYPQKIDLL LPYLSRVIEE LGDPRARSSM AWILGEFSHV IPTSSKLLSE MISTMADEDL
     QIQLALLTAV VKLSLMNGKG NDEELVQKVL NYAINQSSNQ DLRDRAFAYQ RLLTPENVRK
     AQKIVCCEKP SVSYNNNLPE ALLDALLCEI TTLASVYHKL PESFIGQGKF GADAIQRRAV
     EELNIEEANV HEAIEKGANV ENLLDLDFTD PGATSASDSP ITSAQPQSGS NSAMDLFMAF
     EAPSTNNAEP VKARSATDDL LGL