SHOC1_MOUSE
ID SHOC1_MOUSE Reviewed; 1481 AA.
AC A2ALV5;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein shortage in chiasmata 1 ortholog {ECO:0000305};
DE EC=3.6.-.- {ECO:0000250|UniProtKB:Q5VXU9};
DE AltName: Full=Protein ZIP2 homolog {ECO:0000303|PubMed:30272023};
DE Short=MZip2 {ECO:0000303|PubMed:30272023};
GN Name=Shoc1 {ECO:0000303|PubMed:29742103};
GN Synonyms=Zip2 {ECO:0000303|PubMed:30272023};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=30272023; DOI=10.1038/s42003-018-0154-z;
RA Zhang Q., Shao J., Fan H.Y., Yu C.;
RT "Evolutionarily-conserved MZIP2 is essential for crossover formation in
RT mammalian meiosis.";
RL Commun. Biol. 1:147-147(2018).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29742103; DOI=10.1371/journal.pgen.1007381;
RA Guiraldelli M.F., Felberg A., Almeida L.P., Parikh A., de Castro R.O.,
RA Pezza R.J.;
RT "SHOC1 is a ERCC4-(HhH)2-like protein, integral to the formation of
RT crossover recombination intermediates during mammalian meiosis.";
RL PLoS Genet. 14:E1007381-E1007381(2018).
RN [4]
RP INTERACTION WITH SPO16, AND SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
CC -!- FUNCTION: ATPase required during meiosis for the formation of crossover
CC recombination intermediates (PubMed:29742103). Binds DNA:
CC preferentially binds to single-stranded DNA and DNA branched structures
CC (By similarity). Does not show nuclease activity in vitro, but shows
CC ATPase activity, which is stimulated by the presence of single-stranded
CC DNA (By similarity). Plays a key role in homologous recombination and
CC crossing-over in meiotic prophase I in male and female germ cells
CC (PubMed:30272023). Required for recruitment of TEX11 and MSH4 to
CC recombination intermediates (PubMed:30272023).
CC {ECO:0000250|UniProtKB:Q5VXU9, ECO:0000269|PubMed:29742103,
CC ECO:0000269|PubMed:30272023}.
CC -!- SUBUNIT: Interacts with TEX11 (By similarity). Interacts with SPO16
CC (PubMed:30746471). {ECO:0000250|UniProtKB:Q5VXU9,
CC ECO:0000269|PubMed:30746471}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:29742103,
CC ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}.
CC Note=Localizes to meiotic chromosomes; associates with mid-stage
CC meiotic recombination intermediates (PubMed:29742103). Localization
CC requires meiotic double-strand breaks (DSBs) recombination
CC intermediates catalyzed by DMC1 (PubMed:29742103).
CC {ECO:0000269|PubMed:29742103}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in adult testis.
CC {ECO:0000269|PubMed:29742103, ECO:0000269|PubMed:30272023}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic ovaries at embryonic day
CC 16.5. {ECO:0000269|PubMed:30272023}.
CC -!- DISRUPTION PHENOTYPE: Mice show severe defects in meiotic prophase I,
CC such as DNA double-strand break (DSB) repair, crossover formation and
CC synapsis in spermatocytes and oocytes resulting in sterility in both
CC male and females (PubMed:30272023). Embryonic lethality due to defects
CC in meiosis (PubMed:29742103). The use of a hypomorphic allele showed
CC that spermatogenesis progresses normally until the end of prophase I
CC when spermatocytes arrest at metaphase I: homologous chromosomes pair
CC in spermatocytes but show defective synapsis (PubMed:29742103).
CC {ECO:0000269|PubMed:29742103, ECO:0000269|PubMed:30272023}.
CC -!- SIMILARITY: Belongs to the XPF family. Highly divergent. {ECO:0000305}.
CC -!- CAUTION: Although related to the XPF family, the nuclease active site
CC is not conserved. {ECO:0000305|PubMed:29742103}.
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; AL805972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL808112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX001048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS89749.1; -.
DR RefSeq; XP_017175979.1; XM_017320490.1.
DR AlphaFoldDB; A2ALV5; -.
DR STRING; 10090.ENSMUSP00000103171; -.
DR iPTMnet; A2ALV5; -.
DR PhosphoSitePlus; A2ALV5; -.
DR MaxQB; A2ALV5; -.
DR PaxDb; A2ALV5; -.
DR PRIDE; A2ALV5; -.
DR ProteomicsDB; 373551; -.
DR Antibodypedia; 49256; 33 antibodies from 5 providers.
DR Ensembl; ENSMUST00000107547; ENSMUSP00000103171; ENSMUSG00000038598.
DR MGI; MGI:2140313; Shoc1.
DR VEuPathDB; HostDB:ENSMUSG00000038598; -.
DR eggNOG; ENOG502QVCW; Eukaryota.
DR GeneTree; ENSGT00390000013037; -.
DR HOGENOM; CLU_004755_1_0_1; -.
DR InParanoid; A2ALV5; -.
DR OMA; TCNLDTA; -.
DR OrthoDB; 60413at2759; -.
DR TreeFam; TF338326; -.
DR BioGRID-ORCS; 100155; 0 hits in 36 CRISPR screens.
DR ChiTaRS; Shoc1; mouse.
DR PRO; PR:A2ALV5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2ALV5; protein.
DR Bgee; ENSMUSG00000038598; Expressed in animal zygote and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:UniProtKB.
DR InterPro; IPR039991; SHOC1.
DR PANTHER; PTHR35668; PTHR35668; 1.
DR Pfam; PF17825; DUF5587; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Hydrolase; Meiosis; Reference proteome.
FT CHAIN 1..1481
FT /note="Protein shortage in chiasmata 1 ortholog"
FT /id="PRO_0000444881"
FT REGION 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 168065 MW; 00C1AFDA987A7AD2 CRC64;
MALNGRTMFP AFKYYAIDYL QEDIIKERLY RDALLLQIPS CLNQDKNIID DKYRTPWTRA
IPVQEMEDNS VLEQWRTRFC VEGVPEKKTV TGVMINGTFE EIVPSSNPNS PPGIENDKLF
PSKDYVDDFI PVKCSLYYPG VKAEHQGLLI DEEMIFMNKA MDNHLPTVNG LLSRLKLYLV
KDPFLDFKEE LSGKDNFTEY FSVQECSEPF VRDFHMAEET FCKKKLPSVF PSGFKSLIST
NPKQEILILP PSKLKKPLNS IPKIMDSVDE SECFKGDITS KHEFDTEDIK CNSTENLTFA
SLCEPECSEP GDLEMPPTHL ILPRQHSAVS SLHMGFQTFP FSATCKINLL SAGESANKYC
MLWQLGGCRN SWVSFLLTVP RFQEPSSQYS LADMRNIFSV KGDSLVINPA KAKGWRQARL
HPIMAETLAH LKAYLCHNGL SSQETKLEIF LPTKVFQLES WLELKSRPLP IVPISEKSTD
VHQLHPQKRP IPSSEKEVPH LCLSGESISV KKSKVEANPK NDQEPEARIM QKPENSCVGL
GCSSQVPSAE SASSSQIQAS YDKKQDDLDL LSEFIILRSK HQTFPSEADV DVKSHDHDQN
NEFQDKEKYS LTLQEESLVA SNSKAPEERC EERTDGVIEI PASDTQCQAY CLLEATANPI
LKELVCLCTY PAANWKFATV NFDQTRFFLK EQEKKINDAT HPDKNDDRKM TFRHAALLHL
LITIRDVLLT CNLDTALGYL SNAKDIYKSV LDSRLDNIWR QLKILQFIKE KRPKSNYKIQ
ELQCQILSRL QNQQQMKVLI IIRMDSDGEK HLLIKTLKKI EGLTMTVLRS NDRKKILETT
SILKGTNACV VVHNHSIGAD FPWSSFSLVV EYNHVGHSCW AEHCQLLDIP FLAFKVAVPD
TALQRDALLD GFGGFLLKIP IPYVFFASEG LLNTPEILRL LESNYNITLV ERCCCGSLKL
FGSTECYVVV TVDEHTAIVV QDLEELHHEK ASDNIIMRLM ALSFQYSCCW IILYSKETLN
SQYHLTEETL RHLAQVYAAL VSSGLKSEEL DVKLIIAPGV EETALIIRQI ADHNLMTSTR
DPHEWLDKSW VEVSPSKEEM SLLDFPCINP LVAQLMLHRA PSLHWLLIAT PAELQELLPQ
VPGKVLKHFC SITSLFKISS PSMTKSSQIS SLQEDMNQTD LFISQSSAPI IQEQEEYYPY
EDSEGTSSSP VELRATPCML PSAAPHSQRG CWEDPSCGPD PVQNNPSLMN AESKKVTWPS
VPSWSDSESD VFSLARTQVS CEPIMTLTDS QRRGTNGFVN CPEAKGPRNM QVSTPVFLPE
NSQSHLHWDF KKNSCRKQIY SFNPSCGTEQ TTYNKWYSWK DDFSSNQPEC LWDEMEDVTY
RNANAGTRET FWRELPAVPS WDSPCASDSN ANQRGFKGLD FCQRAGNYLG QRSLPVSSSN
WGDYKTPTDL MYSQVPQPKK RRLMYEKVPG RVDGQTRLKF L