HOP1_SCHPO
ID HOP1_SCHPO Reviewed; 528 AA.
AC Q9P7P2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Linear element-associated protein hop1 {ECO:0000312|PomBase:SPBC1718.02};
DE AltName: Full=Meiosis-specific protein hop1;
GN Name=hop1 {ECO:0000312|PomBase:SPBC1718.02};
GN ORFNames=SPBC1718.02 {ECO:0000312|PomBase:SPBC1718.02};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=15226405; DOI=10.1242/jcs.01203;
RA Lorenz A., Wells J.L., Pryce D.W., Novatchkova M., Eisenhaber F.,
RA McFarlane R.J., Loidl J.;
RT "S. pombe meiotic linear elements contain proteins related to synaptonemal
RT complex components.";
RL J. Cell Sci. 117:3343-3351(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=16532353; DOI=10.1007/s00412-006-0053-9;
RA Lorenz A., Estreicher A., Kohli J., Loidl J.;
RT "Meiotic recombination proteins localize to linear elements in
RT Schizosaccharomyces pombe.";
RL Chromosoma 115:330-340(2006).
RN [4]
RP FUNCTION, INTERACTION WITH REC10 AND REC15, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 344-GLU--ASP-370.
RX PubMed=31665745; DOI=10.1093/nar/gkz754;
RA Kariyazono R., Oda A., Yamada T., Ohta K.;
RT "Conserved HORMA domain-containing protein Hop1 stabilizes interaction
RT between proteins of meiotic DNA break hotspots and chromosome axis.";
RL Nucleic Acids Res. 47:10166-10180(2019).
RN [5]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=33825974; DOI=10.1007/s00412-021-00757-w;
RA Ding D.Q., Matsuda A., Okamasa K., Hiraoka Y.;
RT "Linear elements are stable structures along the chromosome axis in fission
RT yeast meiosis.";
RL Chromosoma 130:s00412.021.00757-s00412.021.00757(2021).
CC -!- FUNCTION: Facilitates initiation of meiotic recombination and DNA
CC double-strand break (DSB) formation at DSB hotspot sites by enhancing
CC the interaction between rec10 and rec15. {ECO:0000269|PubMed:31665745}.
CC -!- SUBUNIT: Interacts (via N-terminus) with rec10; the interaction is
CC direct (PubMed:31665745). Interacts (via C-terminus) with rec15 (via C-
CC terminus); the interaction is direct (PubMed:31665745).
CC {ECO:0000269|PubMed:31665745}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15226405,
CC ECO:0000269|PubMed:16532353, ECO:0000269|PubMed:31665745,
CC ECO:0000269|PubMed:33825974}. Chromosome {ECO:0000269|PubMed:15226405,
CC ECO:0000269|PubMed:16532353, ECO:0000269|PubMed:31665745}.
CC Note=Predominantly localizes to linear elements (LinEs) on meiotic
CC chromosomes, the S.pombe equivalents of synaptonemal complexes. A
CC proportion also localizes to DNA double-strand break (DSB) hotspots.
CC {ECO:0000269|PubMed:15226405, ECO:0000269|PubMed:16532353,
CC ECO:0000269|PubMed:31665745}.
CC -!- DEVELOPMENTAL STAGE: Present from pre-meiotic DNA replication and
CC throughout meiosis I. {ECO:0000269|PubMed:33825974}.
CC -!- DISRUPTION PHENOTYPE: Decreases DNA double-strand break formation
CC during meiosis and meiotic gene conversion at ade6 (PubMed:31665745).
CC Decreases localization of rec15 and rec10 to DNA double strand break
CC (DSB) hotspots, and decreases localization of rec15 to chromosomal axis
CC sites (PubMed:31665745). Abnormal sporulation (PubMed:33825974).
CC {ECO:0000269|PubMed:31665745, ECO:0000269|PubMed:33825974}.
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DR EMBL; CU329671; CAB75992.1; -; Genomic_DNA.
DR PIR; T50330; T50330.
DR RefSeq; NP_596448.1; NM_001022367.1.
DR AlphaFoldDB; Q9P7P2; -.
DR BioGRID; 276602; 47.
DR STRING; 4896.SPBC1718.02.1; -.
DR PaxDb; Q9P7P2; -.
DR PRIDE; Q9P7P2; -.
DR EnsemblFungi; SPBC1718.02.1; SPBC1718.02.1:pep; SPBC1718.02.
DR GeneID; 2540064; -.
DR KEGG; spo:SPBC1718.02; -.
DR PomBase; SPBC1718.02; hop1.
DR VEuPathDB; FungiDB:SPBC1718.02; -.
DR eggNOG; KOG1844; Eukaryota.
DR HOGENOM; CLU_517916_0_0_1; -.
DR InParanoid; Q9P7P2; -.
DR OMA; PSRWIAH; -.
DR PRO; PR:Q9P7P2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030998; C:linear element; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; ISS:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061659; F:ubiquitin-like protein ligase activity; ISM:PomBase.
DR GO; GO:0010780; P:meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Meiosis; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..528
FT /note="Linear element-associated protein hop1"
FT /id="PRO_0000353843"
FT DOMAIN 11..212
FT /note="HORMA"
FT ZN_FING 334..385
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 507..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT MUTAGEN 344..370
FT /note="EDSEMFQCERCDGWVHCACYGFESDSD->AAAAMFQCERCDGWVHCACYGFA
FT AAAA: Abolishes binding to rec15. Decreases DNA double-
FT strand break formation during meiosis and meiotic gene
FT conversion at ade6. Decreases localization of hop1, rec15
FT and rec10 to double-strand break (DSB) hotspots, and
FT decreases localization of rec15 to chromosomal axis sites."
FT /evidence="ECO:0000269|PubMed:31665745"
SQ SEQUENCE 528 AA; 61553 MW; C3AFF919C9714235 CRC64;
MNSYKEEILQ TKSDFTLKNL IFFAISTLCY KRALFNENCY KKVNFEIEHF KGADFDCQLK
PTVVSLQAGV DKEADSFLEM MKTYIFSLVS MKVPFTVYLI ISSQCKSILE DDAVEKEIFS
FTINPGSEEK ICCESFVSYQ RSERFVIKLF LSGNVKTECK DEEKVVQIIT KMERFQLSKG
EATKAGVFLN TVETKDCMSW LNRGEFKDIV SFYESNNGIA ISHCSHAFVP ISTEKIMINK
ESSLFDSQEK IDSQLEKFLQ PLKYDEIGST QILDEQSVEK SLSQGKCEKM QNESRGLREI
KNNNPCEEVK KSNWLKKNIS GSDKVDKAEK KKALLNCECG DSTEDSEMFQ CERCDGWVHC
ACYGFESDSD PRQPNQLLCY TCLLVDSESS LYDRMTMLVA YRRAIRCIWA SEYQGFQKLA
ARLNCSYADA KRIEERLVNE NIIYKEKKRK WIYFTNKSPE MVSYLREKYF TPSRWISHLN
FQNYRQENQR VNMRSFLRPE RMEVIERPKK VSKTSNTKET DTMKPLRI
