IHO1_MOUSE
ID IHO1_MOUSE Reviewed; 574 AA.
AC Q6PDM4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Interactor of HORMAD1 protein 1 {ECO:0000303|PubMed:27723721};
DE AltName: Full=Coiled-coil domain-containing protein 36 {ECO:0000312|MGI:MGI:3612242};
GN Name=Iho1 {ECO:0000303|PubMed:27723721, ECO:0000312|MGI:MGI:3612242};
GN Synonyms=Ccdc36 {ECO:0000312|MGI:MGI:3612242};
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 MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-569 AND SER-570, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, INTERACTION WITH HORMAD1 AND REC114, AND
RP IDENTIFICATION IN THE MCD RECOMBINOSOME COMPLEX.
RX PubMed=27723721; DOI=10.1038/ncb3417;
RA Stanzione M., Baumann M., Papanikos F., Dereli I., Lange J., Ramlal A.,
RA Traenkner D., Shibuya H., de Massy B., Watanabe Y., Jasin M., Keeney S.,
RA Toth A.;
RT "Meiotic DNA break formation requires the unsynapsed chromosome axis-
RT binding protein IHO1 (CCDC36) in mice.";
RL Nat. Cell Biol. 18:1208-1220(2016).
RN [4]
RP INTERACTION WITH ANKRD31.
RX PubMed=31000436; DOI=10.1016/j.molcel.2019.03.022;
RA Papanikos F., Clement J.A.J., Testa E., Ravindranathan R., Grey C.,
RA Dereli I., Bondarieva A., Valerio-Cabrera S., Stanzione M., Schleiffer A.,
RA Jansa P., Lustyk D., Fei J.F., Adams I.R., Forejt J., Barchi M.,
RA de Massy B., Toth A.;
RT "Mouse ANKRD31 regulates spatiotemporal patterning of meiotic recombination
RT initiation and ensures recombination between X and Y sex chromosomes.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Required for DNA double-strand breaks (DSBs) formation in
CC unsynapsed regions during meiotic recombination (PubMed:27723721).
CC Probably acts by forming a complex with MEI4 and REC114, which
CC activates DSBs formation in unsynapsed regions, an essential step to
CC ensure completion of synapsis (PubMed:27723721). Not required for
CC HORMAD1 functions in pairing-independent synaptonemal complex
CC formation, ATR recruitment to unsynapsed axes, meiotic silencing of
CC unsynapsed chromatin (MSUC) or meiotic surveillance (PubMed:27723721).
CC {ECO:0000269|PubMed:27723721}.
CC -!- SUBUNIT: Interacts with HORMAD1 (PubMed:27723721). Interacts with
CC REC114 (PubMed:27723721). Part of the MCD recombinosome complex, at
CC least composed of IHO1, REC114 and MEI4 (PubMed:27723721). Interacts
CC with ANKRD31 (PubMed:31000436). {ECO:0000269|PubMed:27723721,
CC ECO:0000269|PubMed:31000436}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:27723721}.
CC Note=Specifically localizes to unsynapsed chromosomal regions during
CC meiosis (PubMed:27723721). Appears on chromatin during preleptotene,
CC when pre-meiotic replication occurs and axes have not yet developed
CC (PubMed:27723721). Remains associated with unsynapsed axesn zygotene,
CC when axes elongate and synapsis begins but disappears from synapsed
CC axes (PubMed:27723721). Localization diverges in the two sexes beyond
CC zygotene (PubMed:27723721). In spermatocytes, synapsis between the
CC largely non-homologous X and Y chromosomes is mostly constrained to
CC their short pseudoautosomal regions (PARs) (PubMed:27723721). At the
CC zygotene-to-pachytene transition, high levels remain on unsynapsed sex
CC chromosome axes but also on PARs (PubMed:27723721). However, by early
CC pachytene disappears from both the synapsed and unsynapsed regions of
CC sex chromosomes (PubMed:27723721). Reaccumulates on unsynapsed axes of
CC sex chromosomes in mid-late pachytene and on desynapsing autosome axes
CC in diplotene, but disappears from chromatin concomitant with axis
CC disassembly after diplotene (PubMed:27723721). In oocytes, disappears
CC from axes after all chromosomes synapsed and is undetectable on
CC chromatin beyond zygotene (PubMed:27723721). Ovarian levels also
CC dramatically decrease as oocytes progress to late prophase
CC (PubMed:27723721). HORMAD1 is required for robust accumulation on
CC chromatin and unsynapsed axes, suggesting that HORMAD1 recruits IHO1 to
CC unsynapsed axes (PubMed:27723721). {ECO:0000269|PubMed:27723721}.
CC -!- TISSUE SPECIFICITY: Detected in spermatocytes and testis (at protein
CC level) (PubMed:27723721). {ECO:0000269|PubMed:27723721}.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific. {ECO:0000305|PubMed:27723721}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally without obvious somatic
CC defects but males and females are sterile due to defects in homologous
CC synapsis (PubMed:27723721). Oocytes are depleted in six-week-old
CC females and spermatocytes in males undergo apoptosis at a stage
CC equivalent to wild-type mid-pachytene (PubMed:27723721). Complete
CC synapsis is never observed and incomplete synaptonemal complexes are
CC detected in meiocytes equivalent to late-zygotene and pachytene
CC (PubMed:27723721). {ECO:0000269|PubMed:27723721}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58624.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC058624; AAH58624.1; ALT_INIT; mRNA.
DR CCDS; CCDS57701.1; -.
DR RefSeq; NP_001128670.1; NM_001135198.1.
DR RefSeq; XP_006511823.1; XM_006511760.1.
DR RefSeq; XP_006511827.1; XM_006511764.1.
DR AlphaFoldDB; Q6PDM4; -.
DR SMR; Q6PDM4; -.
DR BioGRID; 241805; 2.
DR STRING; 10090.ENSMUSP00000075898; -.
DR iPTMnet; Q6PDM4; -.
DR PhosphoSitePlus; Q6PDM4; -.
DR PaxDb; Q6PDM4; -.
DR PRIDE; Q6PDM4; -.
DR ProteomicsDB; 266960; -.
DR Antibodypedia; 48985; 194 antibodies from 22 providers.
DR Ensembl; ENSMUST00000076592; ENSMUSP00000075898; ENSMUSG00000047220.
DR GeneID; 434438; -.
DR KEGG; mmu:434438; -.
DR UCSC; uc009rpl.2; mouse.
DR CTD; 339834; -.
DR MGI; MGI:3612242; Iho1.
DR VEuPathDB; HostDB:ENSMUSG00000047220; -.
DR eggNOG; ENOG502S0PR; Eukaryota.
DR GeneTree; ENSGT00390000012418; -.
DR HOGENOM; CLU_034910_0_0_1; -.
DR InParanoid; Q6PDM4; -.
DR OMA; PGEFGVW; -.
DR OrthoDB; 974040at2759; -.
DR PhylomeDB; Q6PDM4; -.
DR TreeFam; TF337135; -.
DR BioGRID-ORCS; 434438; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ccdc36; mouse.
DR PRO; PR:Q6PDM4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6PDM4; protein.
DR Bgee; ENSMUSG00000047220; Expressed in mandible and 51 other tissues.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0060629; P:regulation of homologous chromosome segregation; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR031529; IHO1.
DR PANTHER; PTHR35662; PTHR35662; 1.
DR Pfam; PF15771; IHO1; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Differentiation; DNA recombination; Meiosis;
KW Oogenesis; Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..574
FT /note="Interactor of HORMAD1 protein 1"
FT /id="PRO_0000302876"
FT REGION 113..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 217..240
FT /evidence="ECO:0000255"
FT COMPBIAS 114..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..445
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 574 AA; 63340 MW; FACFC1CDC95B6FDB CRC64;
MNFNVWNVKE MLSIPSGSGI TKPSNWNNNQ TDCSLSDSQF LFGSQFCPEN SETLLPSLDA
GACLRHPKQT QQNSVDSEPS IFIKYQAKPQ LLGGDTKDES LFSLPLPVGK SKGLSKQFEE
KKRRATDQSD SETLHSFVSH FPEVINKLQT SVEKTEENLS SRSQSILDSV ETIAKTFQET
ARVQHDLMVE SVRDKGSMEQ AILEIQRTCA ARQAEFMEMK STLKNLEVLV VEQTKNLQQF
CDNLSQLIVP GILEELKKFT SVPQVAGHLK DSTSQTSPSL TQSLHFTRQE KHPSEEPATW
QAQEAPAGNP STSSQRPGEC GVWDEGAESG VFQKAALPTD GLHRGDGHVK NKTVPTYCKN
WVMTTRSVSN HFSNLPSQRA GNGQGLMAQG ASQRDVSKFE ARVKNACPEY GPQSMCSFDS
LEQSATEQKG RPCRKRRRGK KQQPQRSKRG GLLDRKQGQT SKAACAFIAR HHCPQSPVCD
PQGPLICWLT PRSSTKSTCH ILGGTGETSQ TARAAQGNLV QHSQRSSTDS SSQGDQQINW
FSDLSLENLE PPQCKKGGTN LLCDPDFDSS DDNF
