MCAF2_MOUSE
ID MCAF2_MOUSE Reviewed; 452 AA.
AC Q3UL97; Q3UT16; Q4VIF3; Q8BPC5; Q9D4T8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Activating transcription factor 7-interacting protein 2;
DE AltName: Full=MBD1-containing chromatin-associated factor 2;
DE AltName: Full=Protein similar to MCAF2;
GN Name=Atf7ip2; Synonyms=Mcaf2, Psm2;
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 [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=16850184; DOI=10.1007/s11033-006-0001-z;
RA Cai H., Hu J., Song P., Gong W.;
RT "PSM2, a novel protein similar to MCAF2, is involved in the mouse embryonic
RT and adult male gonad development.";
RL Mol. Biol. Rep. 33:159-166(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Egg, Ovary, Testis, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Recruiter that couples transcriptional factors to general
CC transcription apparatus and thereby modulates transcription regulation
CC and chromatin formation. Can both act as an activator or a repressor
CC depending on the context. Mediates MBD1-dependent transcriptional
CC repression, probably by recruiting complexes containing SETDB1. The
CC complex formed with MBD1 and SETDB1 represses transcription and
CC probably couples DNA methylation and histone H3 'Lys-9' trimethylation
CC (H3K9me3) activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MBD1, SETDB1 and SP1. Probably forms a complex
CC with SETDB1 and MBD1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3UL97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UL97-2; Sequence=VSP_024048, VSP_024049;
CC Name=3;
CC IsoId=Q3UL97-3; Sequence=VSP_024046, VSP_024047;
CC Name=4;
CC IsoId=Q3UL97-4; Sequence=VSP_024044, VSP_024045;
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16850184}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early mouse embryo, especially in the
CC embryonic gonad from 11.5 dpc. Continuously expressed from newborn
CC testis to adult. {ECO:0000269|PubMed:16850184}.
CC -!- SIMILARITY: Belongs to the MCAF family. {ECO:0000305}.
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DR EMBL; AY903215; AAX99226.1; -; mRNA.
DR EMBL; AK016180; BAB30138.1; -; mRNA.
DR EMBL; AK077229; BAC36698.1; -; mRNA.
DR EMBL; AK139862; BAE24164.1; -; mRNA.
DR EMBL; AK145634; BAE26553.1; -; mRNA.
DR CCDS; CCDS49758.1; -. [Q3UL97-1]
DR CCDS; CCDS49759.1; -. [Q3UL97-3]
DR RefSeq; NP_083529.1; NM_029253.1. [Q3UL97-3]
DR RefSeq; NP_694763.2; NM_153123.2. [Q3UL97-1]
DR AlphaFoldDB; Q3UL97; -.
DR SMR; Q3UL97; -.
DR STRING; 10090.ENSMUSP00000036731; -.
DR PhosphoSitePlus; Q3UL97; -.
DR PaxDb; Q3UL97; -.
DR PRIDE; Q3UL97; -.
DR ProteomicsDB; 287323; -. [Q3UL97-1]
DR ProteomicsDB; 287324; -. [Q3UL97-2]
DR ProteomicsDB; 287325; -. [Q3UL97-3]
DR ProteomicsDB; 287326; -. [Q3UL97-4]
DR Antibodypedia; 52153; 88 antibodies from 17 providers.
DR DNASU; 75329; -.
DR Ensembl; ENSMUST00000044005; ENSMUSP00000036731; ENSMUSG00000039200. [Q3UL97-1]
DR Ensembl; ENSMUST00000100191; ENSMUSP00000097766; ENSMUSG00000039200. [Q3UL97-4]
DR Ensembl; ENSMUST00000117220; ENSMUSP00000113573; ENSMUSG00000039200. [Q3UL97-2]
DR Ensembl; ENSMUST00000119023; ENSMUSP00000113480; ENSMUSG00000039200. [Q3UL97-3]
DR GeneID; 75329; -.
DR KEGG; mmu:75329; -.
DR UCSC; uc007ydf.2; mouse. [Q3UL97-3]
DR UCSC; uc007ydh.2; mouse. [Q3UL97-2]
DR UCSC; uc007ydi.2; mouse. [Q3UL97-1]
DR CTD; 80063; -.
DR MGI; MGI:1922579; Atf7ip2.
DR VEuPathDB; HostDB:ENSMUSG00000039200; -.
DR eggNOG; ENOG502S2DM; Eukaryota.
DR GeneTree; ENSGT00530000063707; -.
DR HOGENOM; CLU_025197_0_0_1; -.
DR InParanoid; Q3UL97; -.
DR OMA; CHENPSN; -.
DR OrthoDB; 646436at2759; -.
DR PhylomeDB; Q3UL97; -.
DR TreeFam; TF329427; -.
DR BioGRID-ORCS; 75329; 3 hits in 70 CRISPR screens.
DR PRO; PR:Q3UL97; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3UL97; protein.
DR Bgee; ENSMUSG00000039200; Expressed in spermatocyte and 69 other tissues.
DR ExpressionAtlas; Q3UL97; baseline and differential.
DR Genevisible; Q3UL97; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR026085; ATF7-int.
DR InterPro; IPR026089; ATF7-int_2.
DR InterPro; IPR031870; ATF7IP_BD.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR23210; PTHR23210; 2.
DR PANTHER; PTHR23210:SF23; PTHR23210:SF23; 2.
DR Pfam; PF16788; ATF7IP_BD; 1.
DR Pfam; PF16794; fn3_4; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..452
FT /note="Activating transcription factor 7-interacting
FT protein 2"
FT /id="PRO_0000281785"
FT DOMAIN 346..450
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 185..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U623"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U623"
FT VAR_SEQ 204..225
FT /note="GRKTNLPSTCVEFASESNTDDV -> AGFENCGQSPDQFLVPNNSLLT (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024044"
FT VAR_SEQ 226..452
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024045"
FT VAR_SEQ 288..300
FT /note="ESPSFTLKSTSKA -> GKGCFYIFLSKCM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024046"
FT VAR_SEQ 301..452
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024047"
FT VAR_SEQ 317..319
FT /note="GFG -> VLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16850184"
FT /id="VSP_024048"
FT VAR_SEQ 320..452
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16850184"
FT /id="VSP_024049"
FT CONFLICT 18
FT /note="M -> V (in Ref. 1; AAX99226)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="S -> G (in Ref. 1; AAX99226)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="I -> V (in Ref. 1; AAX99226)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="R -> T (in Ref. 2; BAE24164)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..233
FT /note="KNS -> NFF (in Ref. 2; BAB30138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50975 MW; 55CC59FCAE6F7422 CRC64;
MESPDRKRQK VLKAKKTMPT SYQKQLEILN KSTNVEAPKT TVGTNIPNGH NQKMFSKNKE
NVKVMKVSEQ INENACGALE RHTALLEQVK HWIRQEICMI NCNLFDKKLN ELNERIGKTQ
CKSRHEAIAG ELFVKIRRLQ KRIKTVLSSQ RNCLEPNTLP SNTVCKVTDS EAMNLNVTQK
SVKSRSKRIS SVNHTPLNSS EKAGRKTNLP STCVEFASES NTDDVMLISV KNSNLTTSIT
SEQTEIRKNT SRNLSNSPNS MIKVGPVEKK FDFVIDLTRE GPSNYSIESP SFTLKSTSKA
VLRSKEIIPV AENGNEGFGS FEHLPPLPEP PAPLPEMADK IKDTLPPQKP ELKVKWVLRP
TSIALTWNIP KVNPNCAPVE SYHLFLYYEN SDHLTWKKIA EIKALPLPMA CTLSQNLAST
KYYFAVQSKD IFGRYGPFCN IKSIPRFSEN LT
