HCFC2_MOUSE
ID HCFC2_MOUSE Reviewed; 722 AA.
AC Q9D968; G5E837;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Host cell factor 2;
DE Short=HCF-2;
DE AltName: Full=C2 factor;
GN Name=Hcfc2;
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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] {ECO:0000312|EMBL:EDL21371.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 461-722.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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).
RN [4]
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 [5]
RP INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
RN [6]
RP STRUCTURE BY NMR OF 607-716.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of C-terminal fibronectin type III domain of mouse
RT 1700129l13rik protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- SUBUNIT: Binds KMT2A/MLL1. Component of the MLL1/MLL complex, at least
CC composed of KMT2A/MLL1, ASH2L, RBBP5, DPY30, WDR5, MEN1, HCFC1 and
CC HCFC2 (By similarity). Interacts with TASOR (PubMed:31112734).
CC {ECO:0000250|UniProtKB:Q9Y5Z7, ECO:0000269|PubMed:31112734}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5Z7}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y5Z7}.
CC -!- TISSUE SPECIFICITY: Expressed in the spermatogonia, spermatocytes and
CC ovary. {ECO:0000269|PubMed:31112734}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24953.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC152980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466539; EDL21371.1; -; Genomic_DNA.
DR EMBL; AK007317; BAB24953.1; ALT_INIT; mRNA.
DR CCDS; CCDS36014.1; -.
DR RefSeq; NP_001074687.1; NM_001081218.1.
DR PDB; 1WFT; NMR; -; A=607-716.
DR PDBsum; 1WFT; -.
DR AlphaFoldDB; Q9D968; -.
DR BMRB; Q9D968; -.
DR SMR; Q9D968; -.
DR STRING; 10090.ENSMUSP00000020478; -.
DR iPTMnet; Q9D968; -.
DR PhosphoSitePlus; Q9D968; -.
DR EPD; Q9D968; -.
DR MaxQB; Q9D968; -.
DR PaxDb; Q9D968; -.
DR PeptideAtlas; Q9D968; -.
DR PRIDE; Q9D968; -.
DR ProteomicsDB; 269768; -.
DR ProteomicsDB; 330546; -.
DR Antibodypedia; 1771; 170 antibodies from 21 providers.
DR DNASU; 67933; -.
DR Ensembl; ENSMUST00000020478; ENSMUSP00000020478; ENSMUSG00000020246.
DR GeneID; 67933; -.
DR KEGG; mmu:67933; -.
DR UCSC; uc007gjt.1; mouse.
DR CTD; 29915; -.
DR MGI; MGI:1915183; Hcfc2.
DR VEuPathDB; HostDB:ENSMUSG00000020246; -.
DR eggNOG; KOG4152; Eukaryota.
DR GeneTree; ENSGT00940000160733; -.
DR HOGENOM; CLU_002603_1_0_1; -.
DR InParanoid; Q9D968; -.
DR OMA; GWIPVPE; -.
DR OrthoDB; 416932at2759; -.
DR TreeFam; TF314757; -.
DR BioGRID-ORCS; 67933; 9 hits in 75 CRISPR screens.
DR ChiTaRS; Hcfc2; mouse.
DR EvolutionaryTrace; Q9D968; -.
DR PRO; PR:Q9D968; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D968; protein.
DR Bgee; ENSMUSG00000020246; Expressed in seminiferous tubule of testis and 234 other tissues.
DR ExpressionAtlas; Q9D968; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; ISO:MGI.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR043536; HCF1/2.
DR InterPro; IPR037932; HCF2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR PANTHER; PTHR46003; PTHR46003; 2.
DR PANTHER; PTHR46003:SF2; PTHR46003:SF2; 2.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kelch repeat; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..722
FT /note="Host cell factor 2"
FT /id="PRO_0000119073"
FT REPEAT 34..79
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 83..130
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 207..255
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 257..303
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT DOMAIN 359..460
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 514..604
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 606..716
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 398..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 708..722
FT /note="VRWLQDQEKDVGPWF -> IRWLQGNSKKAPLS (in Ref. 3;
FT BAB24953)"
FT /evidence="ECO:0000305"
FT STRAND 611..617
FT /evidence="ECO:0007829|PDB:1WFT"
FT STRAND 619..627
FT /evidence="ECO:0007829|PDB:1WFT"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:1WFT"
FT STRAND 658..666
FT /evidence="ECO:0007829|PDB:1WFT"
FT STRAND 668..673
FT /evidence="ECO:0007829|PDB:1WFT"
FT HELIX 674..677
FT /evidence="ECO:0007829|PDB:1WFT"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1WFT"
FT STRAND 689..702
FT /evidence="ECO:0007829|PDB:1WFT"
FT STRAND 706..711
FT /evidence="ECO:0007829|PDB:1WFT"
SQ SEQUENCE 722 AA; 79435 MW; C1820F08C5EB07FA CRC64;
MAAPSLLNWR RVSSFTGPVP RARHGHRAVA IRELMIIFGG GNEGIADELH VYNTVTNQWF
LPAVRGDIPP GCAAHGFVCD GTRILVFGGM VEYGRYSNEL YELQASRWLW KKVKPQPPPS
GFPPCPRLGH SFSLYGNKCY LFGGLANESE DSNNNVPRYL NDFYELELQH GSGVVGWSIP
ATKGVVPSPR ESHTAIIYCK KDSASPKMYV FGGMCGARLD DLWQLDLETM SWSKPETKGT
VPLPRSLHTA SVIGNKMYIF GGWVPHKGEN PETSPHDCEW RCTSSFSYLN LDTAEWTTLV
SDSQEDKKNS RPRPRAGHCA VAIGTRLYFW SGRDGYKKAL NSQVCCKDLW YLDTEKPPAP
SQVQLIKATT NSFHVKWDEV PTVEGYLLQL NTDLTYQATS SDSSAAPSVL GGRMDPHRQG
SNSTLHNSVS DTVNSTKTEH TAVRGTSLRS KPDSRAVDSS AALHSPLAPN TSNNSSWVTD
MLRKNEVDEI CALPATKISR VEVHAAATPF SKETPSNPVA ILKAEQWCDV GIFKNNTALV
SQFYLLPKGK QSMSKVGNAD VPDYSLLKKQ DLVPGTVYKF RVAAINGCGI GPLSKVSEFK
TCTPGFPGAP STVRISKNVD GIHLSWEPPT SPSGNILEYS AYLAIRTAQM QDNPSQLVFM
RIYCGLKTSC TVTAGQLANA HIDYTSRPAI VFRISAKNEK GYGPATQVRW LQDQEKDVGP
WF
