(data stored in ACNUC22857 zone)

SWISSPROT: AP2B_SCHPO

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   05-JUL-2017, entry version 103.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
CC       link clathrin to receptors in coated vesicles. Clathrin-associated
CC       protein complexes are believed to interact with the cytoplasmic
CC       tails of membrane proteins, leading to their selection and
CC       concentration. Beta adaptin is a subunit of the plasma membrane
CC       adaptor (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC       composed of two large adaptins (alpha-type subunit apl3 and beta-
CC       type subunit apl1), a medium chain (mu-type subunit apm4) and a
CC       small adaptin (sigma-type subunit aps2). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane,
CC       coated pit {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of
CC       the coat surrounding the cytoplasmic face of coated vesicles in
CC       the plasma membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
DR   EMBL; CU329671; CAA17886.1; -; Genomic_DNA.
DR   PIR; T40145; T40145.
DR   RefSeq; NP_596435.1; NM_001022354.2.
DR   ProteinModelPortal; O43005; -.
DR   SMR; O43005; -.
DR   BioGrid; 276904; 6.
DR   MINT; MINT-4674566; -.
DR   STRING; 4896.SPBC2G2.06c.1; -.
DR   MaxQB; O43005; -.
DR   PRIDE; O43005; -.
DR   EnsemblFungi; SPBC2G2.06c.1; SPBC2G2.06c.1:pep; SPBC2G2.06c.
DR   GeneID; 2540375; -.
DR   KEGG; spo:SPBC2G2.06c; -.
DR   EuPathDB; FungiDB:SPBC2G2.06c; -.
DR   PomBase; SPBC2G2.06c; apl1.
DR   HOGENOM; HOG000163270; -.
DR   InParanoid; O43005; -.
DR   OMA; MSNNDMV; -.
DR   OrthoDB; EOG092C18N0; -.
DR   PhylomeDB; O43005; -.
DR   Reactome; R-SPO-8856825; Cargo recognition for 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; IDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IC:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
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;
DR   PRODOM; O43005.
DR   SWISS-2DPAGE; O43005.
KW   Cell membrane; Coated pit; Complete proteome; Endocytosis; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN         1    677       AP-2 complex subunit beta.
FT                                /FTId=PRO_0000193754.
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
//

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