ID   AP3B_SCHPO              Reviewed;         745 AA.
AC   O13939;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=AP-3 complex subunit beta;
DE   AltName: Full=Adaptor-related protein complex 3 subunit beta;
DE   AltName: Full=Beta-3-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 3 beta large chain;
DE   AltName: Full=Clathrin assembly protein large beta chain;
GN   Name=apl6; ORFNames=SPAC23H3.06;
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-638, 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. Beta
CC       adaptin is a subunit of the plasma membrane adaptor (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC       of 2 large adaptins (apl5 and apl6), a medium adaptin (apm3) and a
CC       small adaptin (aps3). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P46682}.
CC       Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC       {ECO:0000250|UniProtKB:P46682}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P46682}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P46682}. Note=Component of the coat surrounding
CC       the cytoplasmic face of coated vesicles located at the Golgi complex.
CC       {ECO:0000250|UniProtKB:P46682}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB16234.1; -; Genomic_DNA.
DR   PIR; T38299; T38299.
DR   RefSeq; NP_593796.1; NM_001019225.2.
DR   AlphaFoldDB; O13939; -.
DR   SMR; O13939; -.
DR   BioGRID; 278265; 27.
DR   IntAct; O13939; 1.
DR   STRING; 4896.SPAC23H3.06.1; -.
DR   iPTMnet; O13939; -.
DR   MaxQB; O13939; -.
DR   PaxDb; O13939; -.
DR   PRIDE; O13939; -.
DR   EnsemblFungi; SPAC23H3.06.1; SPAC23H3.06.1:pep; SPAC23H3.06.
DR   GeneID; 2541771; -.
DR   KEGG; spo:SPAC23H3.06; -.
DR   PomBase; SPAC23H3.06; apl6.
DR   VEuPathDB; FungiDB:SPAC23H3.06; -.
DR   eggNOG; KOG1060; Eukaryota.
DR   HOGENOM; CLU_006320_3_2_1; -.
DR   InParanoid; O13939; -.
DR   OMA; IGRCAQS; -.
DR   PhylomeDB; O13939; -.
DR   PRO; PR:O13939; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030123; C:AP-3 adaptor complex; ISO:PomBase.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0006896; P:Golgi to vacuole transport; ISO:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:PomBase.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR026740; AP3_beta.
DR   InterPro; IPR026739; AP_beta.
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   PANTHER; PTHR11134:SF1; PTHR11134:SF1; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..745
FT                   /note="AP-3 complex subunit beta"
FT                   /id="PRO_0000193756"
FT   REGION          674..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..712
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         638
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   745 AA;  83871 MW;  D90D274032BA0A47 CRC64;
     MSNLSFFQTL SGLAENAKQI AKSSSLSFEE NELSHSDLLR LLNSNSDAGK LEAINFILAQ
     MMHGENMSLY FPDVVKLVAS ENPEIRRLVH IYLLQYAEFN PDLALLSVNT VQKTLYDKNP
     LTRSTAIRVM SSIRVPAING IVLLAIQQCI TDTADRVRQS AALAITKCYS LDPSYKSQLE
     EHIKTLLSDN SPIVVPAALF TFEVVCPEKL EIIHPYYHRI CTLFPQMNDW DKVVALKTLV
     RYARLTLPEP STPSTHSDLK ELLESIKSCF FSLLPSTIIA GARAFYYLAP SNQMHLIVEP
     LLQLLLEKPI VRTTTLRYIS QIVYKTPELF KNHIKSFFLI ASDSDDTCLL KINILSRLLD
     AQNSSQILPE LLYYINSHPN PSVASTAVKA LGDFASANIS MAPSCLNTLL LLLKSHNSLI
     VTEAASSLRL LIHNDPKEIY LQYLAATYET LEVPRAKSVT LWLISEHILI IPRLVPDVLR
     IAVKTFADET LEVKYQILEL SVRLYVLSHS EEKQNDLESR DDVVSLLFNY VLSLIHFDMS
     YDLRDRARFY KELASTPSSE FTRRIVLESK GNSQKEIIAS RDYCIGTASL CLNEDVMGYE
     PIPNWADVSD LPPDSVREGI KDVLPINPHT GNIYSNNSPG VKALSSDNFK RDFGDTNAIN
     RPKFVGQQTL EEFYASETSE SSEGEYETST SESEDEETDD TSQEEDNEKN STPDEDTENN
     NTSSISTKSI MDRPLTEPEP NYWQS