LAA1_YEAST
ID LAA1_YEAST Reviewed; 2014 AA.
AC P39526; D6VVY7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=AP-1 accessory protein LAA1;
DE AltName: Full=Large AP-1 accessory protein 1;
GN Name=LAA1; OrderedLocusNames=YJL207C; ORFNames=HRD550, J0312;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754713; DOI=10.1002/yea.320100912;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT homologues to chromosome III genes.";
RL Yeast 10:1235-1249(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1465-2014.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7725802; DOI=10.1002/yea.320101216;
RA Vandenbol M., Durand P., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequence analysis of a 40.2 kb DNA fragment located near the left telomere
RT of yeast chromosome X.";
RL Yeast 10:1657-1662(1994).
RN [5]
RP DRUG SENSITIVITY.
RX PubMed=10407277;
RX DOI=10.1002/(sici)1097-0061(199907)15:10b<973::aid-yea402>3.0.co;2-l;
RA Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P.,
RA Maundrell K.;
RT "Chemotyping of yeast mutants using robotics.";
RL Yeast 15:973-986(1999).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [9]
RP FUNCTION, INTERACTION WITH AP-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16687571; DOI=10.1091/mbc.e06-02-0096;
RA Fernandez G.E., Payne G.S.;
RT "Laa1p, a conserved AP-1 accessory protein important for AP-1 localization
RT in yeast.";
RL Mol. Biol. Cell 17:3304-3317(2006).
CC -!- FUNCTION: Involved in the trans-Golgi network (TGN)-endosome transport.
CC Important for the correct localization of the adapter protein complex
CC AP-1. {ECO:0000269|PubMed:16687571}.
CC -!- SUBUNIT: Interacts with the clathrin-associated adapter complex AP-1.
CC {ECO:0000269|PubMed:16687571}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16687571, ECO:0000269|PubMed:16702403}.
CC Note=Colocalizes with AP-1 adapter complex, with clathrin-coated
CC vesicles to the late-Golgi apparatus and with ribosomes. Localization
CC depends on ADP-ribosylation factor (ARF).
CC -!- DISRUPTION PHENOTYPE: Deletion, when combined with a conditional
CC mutation in clathrin heavy chain or deletion of GGA genes, accentuates
CC growth defects and increases disruption of clathrin-dependent alpha-
CC factor maturation and transport of carboxypeptidase Y to the vacuole.
CC Causes mislocalization of AP-1, especially in cells at high density
CC (postdiauxic shift), but doesn't affect GGA protein distribution.
CC Sensitive to diltiazem-HCl and hypersensitive to chlorpromazine.
CC {ECO:0000269|PubMed:16687571}.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X77688; CAA54749.1; -; Genomic_DNA.
DR EMBL; Z34098; CAA84004.1; -; Genomic_DNA.
DR EMBL; Z49482; CAA89504.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08603.1; -; Genomic_DNA.
DR PIR; S46622; S46622.
DR RefSeq; NP_012328.1; NM_001181640.1.
DR AlphaFoldDB; P39526; -.
DR BioGRID; 33551; 38.
DR DIP; DIP-6552N; -.
DR IntAct; P39526; 21.
DR MINT; P39526; -.
DR STRING; 4932.YJL207C; -.
DR iPTMnet; P39526; -.
DR MaxQB; P39526; -.
DR PaxDb; P39526; -.
DR PRIDE; P39526; -.
DR EnsemblFungi; YJL207C_mRNA; YJL207C; YJL207C.
DR GeneID; 853223; -.
DR KEGG; sce:YJL207C; -.
DR SGD; S000003743; LAA1.
DR VEuPathDB; FungiDB:YJL207C; -.
DR eggNOG; KOG1822; Eukaryota.
DR GeneTree; ENSGT00390000006205; -.
DR HOGENOM; CLU_231814_0_0_1; -.
DR InParanoid; P39526; -.
DR OMA; QLFLFWK; -.
DR BioCyc; YEAST:G3O-31635-MON; -.
DR PRO; PR:P39526; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P39526; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040108; Laa1/Sip1/HEATR5.
DR PANTHER; PTHR21663; PTHR21663; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW Golgi apparatus; Protein transport; Reference proteome; Transport.
FT CHAIN 1..2014
FT /note="AP-1 accessory protein LAA1"
FT /id="PRO_0000203015"
SQ SEQUENCE 2014 AA; 229900 MW; 6A296796F2FA5791 CRC64;
MANRSLKKVI ETSSNNGHDL LTWITTNLEK LICLKEVNDN EIQEVKEIHT QLDEFVRYIS
VLENTDDLEL HSVFISLSQL YTISIWRLKD EYPGVVFDSA AFLTNVLCEE DVSIDDGDTD
PNQKKKKKKS STKKKKYIYS PAKDIACTIL VQLFENFGSS ISSLIPLLFN AIFKNLKKIM
EKSKYYHATF MTTLLQLFNA ILRNSNNDDK ILDPATYAKF SKLSKTVFDS ISTDEKDFSV
TFVSVLIECW TAHFKQTNFI REHSHDIIET IYSRFTEGEI GVYGFANDET RIFTAKSLAE
ILFDYYFSKN ILTLQEVWSI YVKIFLNCDT RDVESGCFES IIHLINLNLL ADNTFLSNSK
YLDIVLSLSG VFSSYEVNNR SMNTLSRYLR YFQHMHEVIL PHLNDSAKTQ MLYYILGCSD
TYQSSSKSDS ASNFKYSIDA KPETQWLTLL QLDFTYVLIS DLGSTFTTEE NTVKEIRDKL
VDLATCEIFT IRVHTVEILK VFLNNCPEYL SETIENSLRA LSTDFKSTGK FIFHKNHGHA
FIIANLIKGA ESDYISYELI MRITVFSTSF IKNNTTSTSS NLYFKGLLCW ILLIGLMNYK
DEQYLKLQIP QLFLFWKVLL THTYTYHDED ELYKNLEIRN HALTCLLTYL SNTTIDKEMA
KQVSYLLTKC SNFNHSIDLK SKNIDNALLH NENRILQVYL KLEKYINSDF NSSLLILIVK
NFSDPNLYTE SSSSVLGSLK DIGNRKVSNK DDMESNIVLE SSINTLLRQN NGFAFGLSSK
ITGDRIVNLS MSSAYKYDES ISGSWPSKDY NWYNIFEVEV SKPISPILSL DSLILLYGSG
SYSQIDRYAP QVTTSLIDSS MELFSSVFPF LNSKIQYSIM ETLNLSMFSK MTTPLRSVAV
AANVCSALHN ALRIMQENNL ELDYSVGQLI IESIKKIQFF NDIFLTKIKA DCVGLLTAAI
ARTLGDEERQ KFLTEQSRIF IKNVADMDEP YLRMFHVLSL ATIFKYNSQY ANFEEYFDVI
FALMRDPHPV VHSWSLKAMH ILLEKHLVID LKTAALLLSS MEELLVQDKY GIYGRSTLRC
NYNRDFNSHV AIGEISRTLT ETVGPNFLEL NTKVLDSFRN ITLSMLISNN ILNSITSIKM
FENIATFKMK NILNYEIFIL ASKSIIKSSI VTGIGSSYFD TTFTGSNELI SRTSSLKGAF
ENFDLLTLLY KLQMEEFFMK EMENLSWRYL ALFPNSGSVK NYFTEWILHT FKRDNHWFDK
LYSIFNMSLG RLFQSYNRDV SALLEVNGLK KSSEKEIKGE EEESIANVNQ LTDTDAGGLD
SENLQWKSRQ IILNLILMLC LESEKYENLL LALSNKIADL IKISFRGSTV RNEGMKLTGL
HILNFVLKNY STMRDPQVPG SSILEQQEAQ ITSALMPAFS KGSSPTVMSF AITVAAEVLA
SNIMPPDKLG RISQLLIDLL GNFKDPNSGI RIGEAIIVTP KAKRKIELAV LDAWAEVVQR
SITSSNDALF SFTRKYWSIL VPLWIISLRE YMMIKYNDND STVQVKNDSK ENSLIEPRST
KIELYEPVWL NFVEALGCTL DSDVQVILAS LNDEELEYFL FILFSQCLEA IVKNIDDHSV
KMQVLPALHN VLKSNLCIKS IFEDDIITEV VEIMDRLIST GDSKEEFLLV DIISDLIIGY
SKCNATPETF LQDIDKLYEL LRLLMTIISE RLPFIKYNVL TSEEDDNEIK ISPTDISLLK
KTFIAFESNI SNFDNMFKVD LYSCLLFIIG KIYECSHREV IIPIILPLFK ALVKALTESE
DEKNIVLLEI FYGSIKDVIY HKLDSKNKVA TILILLSNGY SKLSFQELNQ CANILSEALN
NPATQPIALQ GFKRIISNIF KYPLLQYFMK LVIKRFFQDI QTNDSLSQAS IKTKLIIQFS
EEVIKQDHQK ASLSIALCLS FFAAYHSAYT EKIDNEVASG IVALAKLDKN SFKEAISSTI
SPQQKAIIGS VMEAYVKSQS LGSVEEAFQL KSFD
