AP18A_YEAST
ID AP18A_YEAST Reviewed; 637 AA.
AC P38856; D3DLB0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Clathrin coat assembly protein AP180A;
GN Name=YAP1801; OrderedLocusNames=YHR161C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH CHC1; CLC1 AND
RP PAN1.
RX PubMed=9531549; DOI=10.1083/jcb.141.1.71;
RA Wendland B., Emr S.D.;
RT "Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates
RT protein-protein interactions essential for endocytosis.";
RL J. Cell Biol. 141:71-84(1998).
RN [4]
RP FUNCTION.
RX PubMed=14704157; DOI=10.1093/genetics/165.4.1661;
RA Baggett J.J., D'Aquino K.E., Wendland B.;
RT "The Sla2p talin domain plays a role in endocytosis in Saccharomyces
RT cerevisiae.";
RL Genetics 165:1661-1674(2003).
RN [5]
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 [6]
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).
CC -!- FUNCTION: Involved in endocytosis and clathrin cage assembly.
CC {ECO:0000269|PubMed:14704157, ECO:0000269|PubMed:9531549}.
CC -!- SUBUNIT: Interacts with PAN1 and the clathrin heavy and light chains
CC CHC1 and CLC1. {ECO:0000269|PubMed:9531549}.
CC -!- INTERACTION:
CC P38856; P22137: CHC1; NbExp=2; IntAct=EBI-24811, EBI-4766;
CC P38856; P32521: PAN1; NbExp=4; IntAct=EBI-24811, EBI-12875;
CC -!- SUBCELLULAR LOCATION: Bud {ECO:0000269|PubMed:9531549}. Bud neck
CC {ECO:0000269|PubMed:9531549}. Cell membrane
CC {ECO:0000269|PubMed:9531549}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9531549}; Cytoplasmic side
CC {ECO:0000269|PubMed:9531549}. Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AP180 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U10397; AAB68993.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06854.1; -; Genomic_DNA.
DR PIR; S46771; S46771.
DR RefSeq; NP_012031.1; NM_001179292.1.
DR AlphaFoldDB; P38856; -.
DR SMR; P38856; -.
DR BioGRID; 36595; 110.
DR DIP; DIP-2278N; -.
DR ELM; P38856; -.
DR IntAct; P38856; 17.
DR MINT; P38856; -.
DR STRING; 4932.YHR161C; -.
DR iPTMnet; P38856; -.
DR MaxQB; P38856; -.
DR PaxDb; P38856; -.
DR PRIDE; P38856; -.
DR EnsemblFungi; YHR161C_mRNA; YHR161C; YHR161C.
DR GeneID; 856566; -.
DR KEGG; sce:YHR161C; -.
DR SGD; S000001204; YAP1801.
DR VEuPathDB; FungiDB:YHR161C; -.
DR eggNOG; KOG0251; Eukaryota.
DR GeneTree; ENSGT00950000183068; -.
DR HOGENOM; CLU_025901_0_0_1; -.
DR InParanoid; P38856; -.
DR OMA; VQYCIYA; -.
DR BioCyc; YEAST:G3O-31196-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:P38856; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38856; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:SGD.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IPI:SGD.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; ANTH_dom_sf.
DR InterPro; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR22951; PTHR22951; 1.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Endocytosis; Membrane; Reference proteome.
FT CHAIN 1..637
FT /note="Clathrin coat assembly protein AP180A"
FT /id="PRO_0000202930"
FT DOMAIN 1..126
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 555..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..637
FT /note="Clathrin-binding"
SQ SEQUENCE 637 AA; 71660 MW; 76B36BE11697A8C2 CRC64;
MTTYFKLVKG ATKIKSAPPK QKYLDPILLG TSNEEDFYEI VKGLDSRIND TAWTIVYKSL
LVVHLMIREG SKDVALRYYS RNLEFFDIEN IRGSNGSASG DMRALDRYDN YLKVRCREFG
KIKKDYVRDG YRTLKLNSGN YGSSRNKQHS INIALDHVES LEVQIQALIK NKYTQYDLSN
ELIIFGFKLL IQDLLALYNA LNEGIITLLE SFFELSHHNA ERTLDLYKTF VDLTEHVVRY
LKSGKTAGLK IPVIKHITTK LVRSLEEHLI EDDKTHNTFV PVDSSQGSAG AVVAKSTAQE
RLEQIREQKR ILEAQLKNEQ VAISPALTTV TAAQSYNPFG TDSSMHTNIP MAVANQTQQI
ANNPFVSQTQ PQVMNTPTAH TEPANLNVPE YAAVQHTVNF NPVQDAGVSA QQTGYYSINN
HLTPTFTGAG FGGYSVSQDT TAASNQQVSH SQTGSNNPFA LHNAATIATG NPAHENVLNN
PFSRPNFDEQ NTNMPLQQQI ISNPFQNQTY NQQQFQQQKM PLSSINSVMT TPTSMQGSMN
IPQRFDKMEF QAHYTQNHLQ QQQQQQQQQQ QQQQQQPQQG YYVPATAGAN PVTNITGTVQ
PQNFPFYPQQ QPQPEQSQTQ QPVLGNQYAN NLNLIDM
