ZIP2_YEAST
ID ZIP2_YEAST Reviewed; 704 AA.
AC P53061; D6VV86;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein ZIP2;
DE AltName: Full=Zipping up meiotic chromosomes protein 2;
GN Name=ZIP2; OrderedLocusNames=YGL249W; ORFNames=NRC704;
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 96604 / S288c / FY1679;
RX PubMed=8972578;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1555::aid-yea43>3.0.co;2-q;
RA Coissac E., Maillier E., Robineau S., Netter P.;
RT "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome
RT VII of Saccharomyces cerevisiae.";
RL Yeast 12:1555-1562(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9590170; DOI=10.1016/s0092-8674(00)81164-2;
RA Chua P.R., Roeder G.S.;
RT "Zip2, a meiosis-specific protein required for the initiation of chromosome
RT synapsis.";
RL Cell 93:349-359(1998).
RN [5]
RP FUNCTION.
RX PubMed=10319812; DOI=10.1016/s0092-8674(00)80741-2;
RA San-Segundo P.A., Roeder G.S.;
RT "Pch2 links chromatin silencing to meiotic checkpoint control.";
RL Cell 97:313-324(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZIP3.
RX PubMed=10943844; DOI=10.1016/s0092-8674(00)00029-5;
RA Agarwal S., Roeder G.S.;
RT "Zip3 provides a link between recombination enzymes and synaptonemal
RT complex proteins.";
RL Cell 102:245-255(2000).
RN [7]
RP FUNCTION.
RX PubMed=10848609; DOI=10.1128/mcb.20.13.4838-4848.2000;
RA Bailis J.M., Smith A.V., Roeder G.S.;
RT "Bypass of a meiotic checkpoint by overproduction of meiotic chromosomal
RT proteins.";
RL Mol. Cell. Biol. 20:4838-4848(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11454751; DOI=10.1093/genetics/158.3.1013;
RA Novak J.E., Ross-Macdonald P.B., Roeder G.S.;
RT "The budding yeast Msh4 protein functions in chromosome synapsis and the
RT regulation of crossover distribution.";
RL Genetics 158:1013-1025(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15035982; DOI=10.1016/s0092-8674(04)00249-1;
RA Fung J.C., Rockmill B., Odell M., Roeder G.S.;
RT "Imposition of crossover interference through the nonrandom distribution of
RT synapsis initiation complexes.";
RL Cell 116:795-802(2004).
RN [10]
RP FUNCTION.
RX PubMed=15805472; DOI=10.1101/gad.1293605;
RA Peoples-Holst T.L., Burgess S.M.;
RT "Multiple branches of the meiotic recombination pathway contribute
RT independently to homolog pairing and stable juxtaposition during meiosis in
RT budding yeast.";
RL Genes Dev. 19:863-874(2005).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16740482; DOI=10.1016/j.devcel.2006.04.003;
RA Tsubouchi T., Zhao H., Roeder G.S.;
RT "The meiosis-specific zip4 protein regulates crossover distribution by
RT promoting synaptonemal complex formation together with zip2.";
RL Dev. Cell 10:809-819(2006).
CC -!- FUNCTION: Required for initiation of meiotic chromosome synapsis.
CC Involved in synaptonemal complex formation, a structure that tethers a
CC pair of homologous chromosomes along their lengths and plays a central
CC role in recombination and homolog segregation during meiosis. Required
CC for the normal localization of MSH4 to chromosomes.
CC {ECO:0000269|PubMed:10319812, ECO:0000269|PubMed:10848609,
CC ECO:0000269|PubMed:10943844, ECO:0000269|PubMed:11454751,
CC ECO:0000269|PubMed:15805472, ECO:0000269|PubMed:16740482,
CC ECO:0000269|PubMed:9590170}.
CC -!- SUBUNIT: Interacts with ZIP3. {ECO:0000269|PubMed:10943844}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=localizes to a meiosis
CC specific chromosomal structure called the synaptonemal complex (SC)
CC formed during meiotic prophase.
CC -!- INDUCTION: During meiosis. {ECO:0000269|PubMed:9590170}.
CC -!- SIMILARITY: Belongs to the ZIP2 family. {ECO:0000305}.
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DR EMBL; X94357; CAA64138.1; -; Genomic_DNA.
DR EMBL; Z72771; CAA96969.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07870.1; -; Genomic_DNA.
DR PIR; S61612; S61612.
DR RefSeq; NP_011265.1; NM_001181115.1.
DR PDB; 6BZF; X-ray; 2.29 A; B/D/F/H=499-704.
DR PDB; 6BZG; X-ray; 2.13 A; B=499-704.
DR PDBsum; 6BZF; -.
DR PDBsum; 6BZG; -.
DR AlphaFoldDB; P53061; -.
DR SMR; P53061; -.
DR BioGRID; 33030; 71.
DR ComplexPortal; CPX-1386; Synapsis initiation complex.
DR ComplexPortal; CPX-5441; SPO16:ZIP2.
DR ComplexPortal; CPX-5442; ZZS complex.
DR DIP; DIP-1241N; -.
DR IntAct; P53061; 2.
DR MINT; P53061; -.
DR STRING; 4932.YGL249W; -.
DR iPTMnet; P53061; -.
DR PaxDb; P53061; -.
DR PRIDE; P53061; -.
DR EnsemblFungi; YGL249W_mRNA; YGL249W; YGL249W.
DR GeneID; 852643; -.
DR KEGG; sce:YGL249W; -.
DR SGD; S000003218; ZIP2.
DR VEuPathDB; FungiDB:YGL249W; -.
DR eggNOG; ENOG502S02Z; Eukaryota.
DR HOGENOM; CLU_385036_0_0_1; -.
DR InParanoid; P53061; -.
DR OMA; NTSMIPH; -.
DR BioCyc; YEAST:G3O-30719-MON; -.
DR PRO; PR:P53061; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53061; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0106069; C:synapsis initiation complex; IC:ComplexPortal.
DR GO; GO:0000795; C:synaptonemal complex; IDA:SGD.
DR GO; GO:0000217; F:DNA secondary structure binding; IDA:SGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR GO; GO:0035825; P:homologous recombination; IC:ComplexPortal.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IMP:SGD.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0090173; P:regulation of synaptonemal complex assembly; IC:ComplexPortal.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Chromosomal rearrangement; Chromosome;
KW Chromosome partition; DNA-binding; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..704
FT /note="Protein ZIP2"
FT /id="PRO_0000202706"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:6BZG"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 514..521
FT /evidence="ECO:0007829|PDB:6BZG"
FT STRAND 527..531
FT /evidence="ECO:0007829|PDB:6BZG"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:6BZG"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:6BZG"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6BZG"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 567..576
FT /evidence="ECO:0007829|PDB:6BZG"
FT STRAND 578..586
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 588..593
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 597..604
FT /evidence="ECO:0007829|PDB:6BZG"
FT STRAND 610..618
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 619..633
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 658..667
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 670..678
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 682..685
FT /evidence="ECO:0007829|PDB:6BZG"
FT HELIX 690..701
FT /evidence="ECO:0007829|PDB:6BZG"
SQ SEQUENCE 704 AA; 82816 MW; 171387494869B56E CRC64;
MIIERWEVKL SKCNQNVGGY SVLSGNLKEN IKLGRRAQKY LKELRNLQLK PLKIGGYENC
GTINGEEYFL EVIHITSGRQ KIDVAVGKTW NVTNIENDNK EELQYELFKE KLKVGKQDML
FFSWMKSLSV QLNAPLHQKM TEHGLADDNT RLEWFNIPLL RRSQYRKKVP YPSLRQMSSV
LEVQCSTLTE EKLNFCVGFS DKPLSEWKPQ IFEQTYNRYR LQRISPEKSF KYKSRCSKYN
FKTSSQSWVV KVPEHDQQLN TFEKRYDELF DAQFNKLEFF KIRMKKLKKN KPIEKKNYKI
WCLEKEDLKD LVWDPLKRIC NHSRYAIFEH VTINREAYSI KPLRLTFQKL DSGSLDLIDN
QKKTFGSIKL AMSMPDVKKT ENQSIEESER HDETAIETQE FDENDCLSSK ADINTSLAPQ
KRSFIDNELM SMLVTKKKIK KDKDVSDTGI SSTSYLINSG TYANSHIEIP TSNSVYNGKE
DCSFNNYSVK HSILEEDIEN KCIAVNENKV IENQKVIQSL CKNSHLDLIE QSYFGECDFI
INHSTCVYKI QASRFMQLRN NGSLHYDKAV NDLLTEFQRV IIIVEFSEII QDVDPDLFWK
IKLYLLNSRV DVFFIHETTD FFIDWMKYFI ARWAFSYNDE KEKNIANADI LLDLGFNILL
VRKIFQTYSL EEFFMAIIKE ESKAVKMLTV SQMTRLKKLL TLEW
