ID   ZIP1_YEAST              Reviewed;         875 AA.
AC   P31111; D6VSR5;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Synaptonemal complex protein ZIP1;
GN   Name=ZIP1; OrderedLocusNames=YDR285W; ORFNames=D9819.9;
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=BR1824-3B;
RX   PubMed=7916652; DOI=10.1016/0092-8674(93)90114-6;
RA   Sym M., Engebrecht J.A., Roeder G.S.;
RT   "ZIP1 is a synaptonemal complex protein required for meiotic chromosome
RT   synapsis.";
RL   Cell 72:365-378(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, 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).
CC   -!- FUNCTION: Required for meiotic chromosome synapsis and cell cycle
CC       progression. May act as a molecular zipper to bring homologous
CC       chromosomes in close apposition. ZIP1 may encode the transverse
CC       filaments of the synaptonemal complex.
CC   -!- INTERACTION:
CC       P31111; Q06032: CST9; NbExp=3; IntAct=EBI-29645, EBI-30044;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Synapsed meiotic
CC       chromosomes.
CC   -!- MISCELLANEOUS: Present with 391 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; L06487; AAA35239.1; -; Genomic_DNA.
DR   EMBL; U51031; AAB64474.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12125.1; -; Genomic_DNA.
DR   PIR; S70115; S70115.
DR   RefSeq; NP_010571.1; NM_001180593.1.
DR   AlphaFoldDB; P31111; -.
DR   SMR; P31111; -.
DR   BioGRID; 32338; 98.
DR   ComplexPortal; CPX-1387; Synaptonemal complex.
DR   DIP; DIP-1240N; -.
DR   IntAct; P31111; 4.
DR   MINT; P31111; -.
DR   STRING; 4932.YDR285W; -.
DR   iPTMnet; P31111; -.
DR   PaxDb; 4932-YDR285W; -.
DR   PeptideAtlas; P31111; -.
DR   EnsemblFungi; YDR285W_mRNA; YDR285W; YDR285W.
DR   GeneID; 851879; -.
DR   KEGG; sce:YDR285W; -.
DR   AGR; SGD:S000002693; -.
DR   SGD; S000002693; ZIP1.
DR   VEuPathDB; FungiDB:YDR285W; -.
DR   eggNOG; ENOG502R6M6; Eukaryota.
DR   HOGENOM; CLU_341332_0_0_1; -.
DR   InParanoid; P31111; -.
DR   OMA; NTQRICS; -.
DR   OrthoDB; 2039263at2759; -.
DR   BioCyc; YEAST:G3O-29849-MONOMER; -.
DR   BioGRID-ORCS; 851879; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P31111; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P31111; Protein.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR   GO; GO:0000794; C:condensed nuclear chromosome; NAS:ComplexPortal.
DR   GO; GO:0000795; C:synaptonemal complex; IDA:SGD.
DR   GO; GO:0000802; C:transverse filament; IDA:SGD.
DR   GO; GO:0032184; F:SUMO polymer binding; IPI:SGD.
DR   GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR   GO; GO:0035825; P:homologous recombination; NAS:ComplexPortal.
DR   GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IMP:SGD.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; IMP:SGD.
DR   GO; GO:1990166; P:protein localization to site of double-strand break; IMP:SGD.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   PANTHER; PTHR23159:SF54; CENTROSOMAL PROTEIN 135KDA, ISOFORM B-RELATED; 1.
DR   PANTHER; PTHR23159; CENTROSOMAL PROTEIN 2; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Coiled coil; Meiosis; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..875
FT                   /note="Synaptonemal complex protein ZIP1"
FT                   /id="PRO_0000066584"
FT   REGION          47..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          177..333
FT                   /evidence="ECO:0000255"
FT   COILED          397..438
FT                   /evidence="ECO:0000255"
FT   COILED          456..752
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        738..752
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..810
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        55
FT                   /note="T -> A (in Ref. 1; AAA35239)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   875 AA;  100035 MW;  674F12625CD9DDFD CRC64;
     MSNFFRDSSM GFKPRPNIFA KLRVRDVDSD SSANTVVENS SNCLDVGSSI EGDDTFKKPH
     KTSTEQELIT SMSLSQRNHG YSDDMEIGSP KKTTSTDQYN RILKNDVAAI ENDTDEDFEI
     TEVREVSEGV AKETKESHGD PNDSETTLKD SKMHEYTMTN GKAPLHTSIN NSSTSSNDVL
     LEAFTNTQRI CSNLKQELQK QQQDNAKLKV RLQSYASNSD KINEKVGKYK SCLETLQERI
     ATLTSHKNNQ ETKLKDLRQN HQLYQRRISG FKTSIENLNK TINDLGKNKK EADAELMKKG
     KEIEYLKREL DDCSGQLSEE KIKNSSLIQE MGKNREEMIK SIENFFSEDK AHHLLQFNKF
     EERVHDLFEK KLQKHFDVAK DTLNVGLRNT TVELSSNTET MLKQQYEDIK ENLEQKMSSS
     KDEMAKTINE LSVTQKGLIM GVQEELLTSS GNIQTALVSE MNNTRQELLD DASQTAKNYA
     SLENLVKAYK AEIVQSNEYE ERIKHLESER STLSSQKNQI ISSLGTKEAQ YEDLVKKLEA
     KNIEISQISG KEQSLTEKNE NLSNELKKVQ DQLEKLNNLN ITTKSNYENK ISSQNEIVKA
     LVSENDTLKQ RIQQLVEIKE NEQKDHTTKL EAFQKNNEQL QKLNVEVVQL KAHELELEEQ
     NRHLKNCLEK KETGVEESLS DVKTLKQQVI VLKSEKQDIT AEKLELQDNL ESLEEVTKNL
     QQKVQSQKRE LEQKIKELEE IKNHKRNEPS KKGTQNFTKP SDSPKKNATT SNLFPNNSAA
     IHSPMKKCPK VDHISKSRIN SSKETSKFND EFDLSSSSND DLELTNPSPI QIKPVRGKIK
     KGSNCMKPPI SSRKKLLLVE DEDQSLKISK KRRRK
//