SCD5_YEAST
ID SCD5_YEAST Reviewed; 872 AA.
AC P34758; D6W326;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein SCD5;
DE AltName: Full=Protein FTB1;
GN Name=SCD5; Synonyms=FTB1; OrderedLocusNames=YOR329C;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8688556; DOI=10.1091/mbc.7.2.245;
RA Nelson K.K., Holmer M., Lemmon S.K.;
RT "SCD5, a suppressor of clathrin deficiency, encodes a novel protein with a
RT late secretory function in yeast.";
RL Mol. Biol. Cell 7:245-260(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 204508 / S288c;
RA Wang W., Zheng L., Chan C.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S288c / GRF88;
RA Song J.M., Cheung E., Rabinowitz J.C.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
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 [7]
RP FUNCTION, INTERACTION WITH GLC7, AND MOTIF.
RX PubMed=12356757; DOI=10.1074/jbc.m208471200;
RA Chang J.S., Henry K., Wolf B.L., Geli M., Lemmon S.K.;
RT "Protein phosphatase-1 binding to scd5p is important for regulation of
RT actin organization and endocytosis in yeast.";
RL J. Biol. Chem. 277:48002-48008(2002).
RN [8]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=12956961; DOI=10.1016/s0960-9822(03)00579-7;
RA Henry K.R., D'Hondt K., Chang J.S., Nix D.A., Cope M.J., Chan C.S.,
RA Drubin D.G., Lemmon S.K.;
RT "The actin-regulating kinase Prk1p negatively regulates Scd5p, a suppressor
RT of clathrin deficiency, in actin organization and endocytosis.";
RL Curr. Biol. 13:1564-1569(2003).
RN [9]
RP PHOSPHORYLATION AT THR-416; THR-450 AND THR-490.
RX PubMed=13679512; DOI=10.1091/mbc.e03-06-0362;
RA Huang B., Zeng G., Ng A.Y., Cai M.;
RT "Identification of novel recognition motifs and regulatory targets for the
RT yeast actin-regulating kinase Prk1p.";
RL Mol. Biol. Cell 14:4871-4884(2003).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Regulates both fluid phase and receptor-mediated endocytosis
CC (PubMed:12356757, PubMed:12956961). Involved in vesicular transport at
CC a late stage of the secretory pathway (PubMed:8688556). Regulates actin
CC cytoskeleton organization (PubMed:12356757, PubMed:12956961).
CC {ECO:0000269|PubMed:12356757, ECO:0000269|PubMed:12956961,
CC ECO:0000269|PubMed:8688556}.
CC -!- SUBUNIT: Interacts (via KKVRF motif) with phosphatase GLC7.
CC {ECO:0000269|PubMed:12356757}.
CC -!- INTERACTION:
CC P34758; P32598: GLC7; NbExp=4; IntAct=EBI-16685, EBI-13715;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8688556}; Peripheral
CC membrane protein {ECO:0000269|PubMed:8688556}.
CC -!- PTM: Phosphorylation by PRK1 and/or AKL1 on Thr-416, Thr-450 and Thr-
CC 490 of repeats 1-1, 1-2 and/or 1-3 negatively regulates SCD5 function
CC in endocytosis and actin cytoskeleton organization.
CC {ECO:0000269|PubMed:12956961, ECO:0000269|PubMed:13679512}.
CC -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U03492; AAB09719.1; -; mRNA.
DR EMBL; U42227; AAA85443.1; -; Genomic_DNA.
DR EMBL; Z49821; CAA89976.1; -; Genomic_DNA.
DR EMBL; Z75237; CAA99650.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11092.1; -; Genomic_DNA.
DR PIR; S62061; S62061.
DR RefSeq; NP_014974.3; NM_001183749.3.
DR AlphaFoldDB; P34758; -.
DR BioGRID; 34714; 57.
DR DIP; DIP-1341N; -.
DR ELM; P34758; -.
DR IntAct; P34758; 6.
DR MINT; P34758; -.
DR STRING; 4932.YOR329C; -.
DR iPTMnet; P34758; -.
DR MaxQB; P34758; -.
DR PaxDb; P34758; -.
DR PRIDE; P34758; -.
DR EnsemblFungi; YOR329C_mRNA; YOR329C; YOR329C.
DR GeneID; 854507; -.
DR KEGG; sce:YOR329C; -.
DR SGD; S000005856; SCD5.
DR VEuPathDB; FungiDB:YOR329C; -.
DR eggNOG; ENOG502QQ7A; Eukaryota.
DR HOGENOM; CLU_016142_0_0_1; -.
DR InParanoid; P34758; -.
DR OMA; YICLRTH; -.
DR BioCyc; YEAST:G3O-33806-MON; -.
DR PRO; PR:P34758; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P34758; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IMP:SGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:SGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:SGD.
DR GO; GO:0009306; P:protein secretion; IMP:SGD.
PE 1: Evidence at protein level;
KW Endocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..872
FT /note="Protein SCD5"
FT /id="PRO_0000097621"
FT REPEAT 405..424
FT /note="1-1"
FT REPEAT 439..458
FT /note="1-2"
FT REPEAT 479..498
FT /note="1-3"
FT REPEAT 534..545
FT /note="2-1"
FT REPEAT 564..575
FT /note="2-2"
FT REPEAT 593..604
FT /note="2-3"
FT REPEAT 608..619
FT /note="2-4"
FT REPEAT 623..634
FT /note="2-5"
FT REPEAT 636..647
FT /note="2-5"
FT REPEAT 650..661
FT /note="2-7"
FT REPEAT 683..694
FT /note="2-8"
FT REPEAT 717..728
FT /note="2-9"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..448
FT /note="3 X 20 AA approximate repeats"
FT REGION 460..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..728
FT /note="9 X 12 AA approximate repeats"
FT REGION 591..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 272..276
FT /note="KKRVK motif; Required for interaction with GLC7,
FT endocytosis and actin cytoskeleton organization"
FT /evidence="ECO:0000269|PubMed:12356757"
FT COMPBIAS 44..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 416
FT /note="Phosphothreonine; by PRK1"
FT /evidence="ECO:0000269|PubMed:13679512"
FT MOD_RES 450
FT /note="Phosphothreonine; by PRK1"
FT /evidence="ECO:0000269|PubMed:13679512"
FT MOD_RES 490
FT /note="Phosphothreonine; by PRK1"
FT /evidence="ECO:0000269|PubMed:13679512"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 872 AA; 97305 MW; C60F5BE8808E1D31 CRC64;
MSFDWLNVPG LDLSSGDQAE KRPSNGLGPP SVSFDFGINT AAPHDSSFWD QGSRSHSDTT
LSYRNNHSNT AADNATNVSS PQKDNPPNGE VRTLSGGDVY AESPEDMQVP LSLSQNQLTH
EEIRTYLRWY HYICLRTHGK LVRLNDVFRF LTNFNLSQKV KDRIVEIFRS CKNALNIGQF
FAVLRLVSRA IIYGILPLRR MILEKAPVPK PRPILSSENH EEVYEEVEDD DSSAKTGDQK
VDFDSFASLL LTGKTTRKRV RRRIKNLNFK SKKVRFSEHI TFQDPPNLNQ ESSNNSEARK
QDPDAEDEDQ DSNNDSPLDF TLPMDQLLKR LYKRRKNSGL VSSLPSEQQE TEEEKKVLED
MKDSLSHFKQ IQTVDSASLP ISSVFLQNGN TLPTSNVNNT TVPQQLPLEP LKPTATGSAN
HLVREEYNQG LHPSNGAIQT GLQPLKPTAT GSANYLMRSH MEQPQSIKPS STPETVTNSG
GLQPLKPTAT GSANYLMKQH ISPSVNNPVS SMFQAQFTNQ SSSPQSTGPA FLNSPNITLP
QSNQQQPYQE VNPTQAKIEP SNISPQHTYS NNVRINNGNI VSMPKVEITG AFPPQNTLPQ
HQQSHLLSPQ NTIPQHQRSQ LISPQNTFTQ NQPILSPQHT YSNNQATMIS PQNTYTNNQQ
QPQHLPPPPP PRAQQQQQGA IVPPQHMYSN VQKQNNLVPT QPSYTNSPSI QSPNFLSPQN
AANSYFQSLL SSSPSPNPTP SNASTVNGNN ASNGISSFQN TSAAMNNTQS HQTYIQQQQQ
QQTQQRIYGG QLSQMQQHPG QLHLNNSDIH SQPNKPNYGM LGQQVHQQQQ QQQQQFPFTA
DVNRSNSSDI LGNLQSLQQQ VDALQIQYNR RP
