ID   CNDG2_DANRE             Reviewed;        1140 AA.
AC   E7FH61; F8W2J6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Condensin-2 complex subunit G2 {ECO:0000305};
DE   AltName: Full=Chromosome-associated protein G2 {ECO:0000305};
DE            Short=CAP-G2 {ECO:0000305};
DE   AltName: Full=Non-SMC condensin II complex subunit G2 {ECO:0000312|Ensembl:ENSDARP00000124705};
GN   Name=ncapg2 {ECO:0000303|PubMed:30609410,
GN   ECO:0000312|ZFIN:ZDB-GENE-070410-100};
GN   ORFNames=zgc:162881 {ECO:0000312|ZFIN:ZDB-GENE-070410-100};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN   [1] {ECO:0000312|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=30609410; DOI=10.1016/j.ajhg.2018.11.017;
RG   Task Force for Neonatal Genomics;
RA   Khan T.N., Khan K., Sadeghpour A., Reynolds H., Perilla Y., McDonald M.T.,
RA   Gallentine W.B., Baig S.M., Davis E.E., Katsanis N.;
RT   "Mutations in NCAPG2 Cause a Severe Neurodevelopmental Syndrome that
RT   Expands the Phenotypic Spectrum of Condensinopathies.";
RL   Am. J. Hum. Genet. 104:94-111(2019).
CC   -!- FUNCTION: Regulatory subunit of the condensin-2 complex, a complex
CC       which establishes mitotic chromosome architecture and is involved in
CC       physical rigidity of the chromatid axis (By similarity). Plays a role
CC       in the embryonic development of the head and kidney structures
CC       (PubMed:30609410). {ECO:0000250|UniProtKB:Q86XI2,
CC       ECO:0000269|PubMed:30609410}.
CC   -!- SUBUNIT: Component of the condensin-2 complex, which contains the smc2
CC       and smc4 heterodimer, and three non SMC subunits that probably regulate
CC       the complex: ncaph2, ncapd3 and ncapg2. {ECO:0000250|UniProtKB:Q86XI2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86XI2}.
CC   -!- DISRUPTION PHENOTYPE: At 3 dpf, mutant animals exhibit cerebellar
CC       hypoplasia, a reduction in the anterior structures, including the optic
CC       tecta, and an increase in cell proliferation in the head
CC       (PubMed:30609410). At 2 dpf, aberrant mitotic cell-cycle progression
CC       and an increase in cell death (PubMed:30609410). At 4 dpf, renal
CC       defects including renal aplasia, hypoplasia and enlargment of the
CC       proximal renal convolution tubule are observed (PubMed:30609410).
CC       Morpholino knockdown results in reduced head size, increased cell
CC       proliferation in the head, increased cell death and increased renal-
CC       tubule diameter (PubMed:30609410). In a double morpholino knockdown
CC       together with nphp1, the increase in renal-tubule diameter is
CC       exacerbated (PubMed:30609410). {ECO:0000269|PubMed:30609410}.
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DR   EMBL; BX248235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX324185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU467647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001082961.3; NM_001089492.3.
DR   RefSeq; XP_005166482.2; XM_005166425.2.
DR   AlphaFoldDB; E7FH61; -.
DR   STRING; 7955.ENSDARP00000078525; -.
DR   PaxDb; E7FH61; -.
DR   PeptideAtlas; E7FH61; -.
DR   Ensembl; ENSDART00000148390; ENSDARP00000124705; ENSDARG00000060023.
DR   GeneID; 100037337; -.
DR   KEGG; dre:100037337; -.
DR   CTD; 54892; -.
DR   ZFIN; ZDB-GENE-070410-100; ncapg2.
DR   eggNOG; KOG1949; Eukaryota.
DR   GeneTree; ENSGT00490000043432; -.
DR   HOGENOM; CLU_008117_0_0_1; -.
DR   InParanoid; E7FH61; -.
DR   OMA; SMRTLGE; -.
DR   OrthoDB; 79594at2759; -.
DR   TreeFam; TF101163; -.
DR   Reactome; R-DRE-2299718; Condensation of Prophase Chromosomes.
DR   PRO; PR:E7FH61; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000060023; Expressed in testis and 26 other tissues.
DR   ExpressionAtlas; E7FH61; baseline and differential.
DR   GO; GO:0000796; C:condensin complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024741; Condensin2_G2.
DR   Pfam; PF12422; Condensin2nSMC; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; DNA condensation; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1140
FT                   /note="Condensin-2 complex subunit G2"
FT                   /id="PRO_0000448939"
FT   REPEAT          460..493
FT                   /note="HEAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
SQ   SEQUENCE   1140 AA;  129093 MW;  07C357E47CB0A232 CRC64;
     MSKRKQFLDS VHHEHVQDFL NFIKLHKDGA DPFDLAEILA ELQKSQRQDL WDRQLKLLQH
     SLTVSPSERW ITGAEEDAGD MEVEVSEEQI QTMAVIEGVT IVSTVSVDAL QEKDNYTTLL
     KCAQMLNAIE SALPLSQTPL QQAIHWLFEC WWRRDLQGKE ELGWTAFLVC LENTVTLDKP
     VSELRRLCSL REVLLSVDFG SEKGQQVIDP LLQCFFRASH IKQEEGKRFL AFLFSWNDNF
     IRMIHETIKN QLQFFPKTLS VHVAEIYFRA WRKASGPFLE EIESACIQDL MQHALLLHRN
     SPVHSKVRQI LTYFHKQKFR EGVDEMLHRL YKPVLWKALK ATNAEVRANA TLLFTEAFPI
     HDPNMSSEMV DQAVQKQLDL LFALLDDPQP LVRSSAVLGV CSVLARCWEV IPSAVITDLL
     EKLILQLAND TSSPDVRCSV FMCMSIILDN SLSHPLMEKL LPALKSSLHD SSEKVRVAFV
     GMLLKIKAAR AAKFWKVCSL EHLLARLEMD SAPVSKRIVN LLFNSFFPVN QPETVWCERC
     VTLIQTNPGA ARKFYQHAYL YTAPANIVKL MLVIRKCLNV CIQNAGDEEF ASSNKENSTL
     LEDVLSVQDT SSMASLLEIL VILWKSVQKS LMANQEAFKY TTAKFGSSLP QYLKIFQEER
     CKAPLILLAS LLPASALPAL RSKVMSHLRS LKAGAAVTTY SQTLECLCSW GQISHIVELI
     ENWLTEAAPV KEQGDEESTG KVHFDVLEES KPDLGLDYLD YMLLRPKTRE CLLTLPLDQM
     RPLHKALNKW KSLLFSSLSG SEVSVAAIET ALRAFIFHGR LCIHLQHKFP EEREFLKSLE
     HSVSWVEKRV LPFLVNSSSD QQLSLSTKIV ESCVTVCKNV LRVSVGDSDF RDHLLQHVAS
     VLQTEKGYMC IPHLLALLTE IAHGCLSQKA EGQEDQLSLT IRILTNIFQK VVEILAHRLR
     KDKEEGQELC CSSEEALHDF LLVTKFTSER SEFMTGVFSS LCAAVIIDIS RPLQKISHVE
     ELLMPETVND LPPLSSTILK VTLGCPAVTR FFLSELSSSI ESEAIDSITQ WAAVTHILTI
     IKESDAFIVE LKDIAGSVRR QIQNYYNSIS ENSDDIQRTI YESTVKMLND VLISCQQTNN