NIPLA_DANRE
ID NIPLA_DANRE Reviewed; 2381 AA.
AC F5HSE3; A2BGN2; F1QYK3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Nipped-B-like protein A;
GN Name=nipbla;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22039349; DOI=10.1371/journal.pbio.1001181;
RA Muto A., Calof A.L., Lander A.D., Schilling T.F.;
RT "Multifactorial origins of heart and gut defects in nipbl-deficient
RT zebrafish, a model of Cornelia de Lange Syndrome.";
RL PLoS Biol. 9:E1001181-E1001181(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
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).
CC -!- FUNCTION: May play a structural role in chromatin. Involved in sister
CC chromatid cohesion, possibly by facilitating the cohesin complex
CC loading. Transcription factor, which may promote cortical neuron
CC migration during brain development by regulating the transcription of
CC crucial genes in this process (By similarity).
CC {ECO:0000250|UniProtKB:Q6KCD5, ECO:0000269|PubMed:22039349}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6KCD5}.
CC -!- DEVELOPMENTAL STAGE: Detected in the early blastula, 2.5 hours post
CC fertilization (hpf), before the onset of zygotic gene expression, and
CC expression progressively increases, reaching a peak at late gastrula
CC stages (9 hpf), before decreasing by 26 hpf. Maternal transcripts are
CC detected throughout the blastoderm. Ubiquitous expression continues
CC until early somitogenesis (12 hpf), after which transcript levels
CC gradually decrease in the trunk (15-18 hpf), with strong expression
CC becoming restricted to the head by 25 hpf.
CC {ECO:0000269|PubMed:22039349}.
CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC required for interaction with chromoshadow domains. This motif requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain (By similarity).
CC {ECO:0000250|UniProtKB:Q6KC79}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM14097.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB630366; BAK23968.1; -; mRNA.
DR EMBL; BX510907; CAM14097.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001233213.1; NM_001246284.1.
DR AlphaFoldDB; F5HSE3; -.
DR SMR; F5HSE3; -.
DR STRING; 7955.ENSDARP00000117955; -.
DR PaxDb; F5HSE3; -.
DR PeptideAtlas; F5HSE3; -.
DR PRIDE; F5HSE3; -.
DR GeneID; 570900; -.
DR KEGG; dre:570900; -.
DR CTD; 570900; -.
DR ZFIN; ZDB-GENE-060526-121; nipbla.
DR eggNOG; KOG1020; Eukaryota.
DR InParanoid; F5HSE3; -.
DR PRO; PR:F5HSE3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0090694; C:Scc2-Scc4 cohesin loading complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0071921; P:cohesin loading; ISS:UniProtKB.
DR GO; GO:0048565; P:digestive tract development; IGI:ZFIN.
DR GO; GO:0035118; P:embryonic pectoral fin morphogenesis; IGI:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IGI:ZFIN.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0003146; P:heart jogging; IMP:ZFIN.
DR GO; GO:0003007; P:heart morphogenesis; IBA:GO_Central.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR033031; Scc2/Nipped-B.
DR PANTHER; PTHR21704; PTHR21704; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 2: Evidence at transcript level;
KW Activator; Cell cycle; Developmental protein; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..2381
FT /note="Nipped-B-like protein A"
FT /id="PRO_0000419686"
FT REPEAT 85..124
FT /note="HEAT 1"
FT REPEAT 1299..1337
FT /note="HEAT 2"
FT REPEAT 1375..1413
FT /note="HEAT 3"
FT REPEAT 1477..1516
FT /note="HEAT 4"
FT REPEAT 1843..1881
FT /note="HEAT 5"
FT REGION 131..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2005..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2228..2271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 552..565
FT /note="PxVxL motif"
FT /evidence="ECO:0000250|UniProtKB:Q6KC79"
FT COMPBIAS 131..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2006..2022
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2253..2269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2381 AA; 268124 MW; 9C949F271A823F5C CRC64;
MNGDMPHVPI TTLAGIAGLT DLLNQLPLPS PLPGTTTKSL LYNGRVAEDV GHLLGCRDET
LVSQLANSLS QVSTEHIELK DSLGSDELEG DVPVLLQLLM SRNPNIFRNK TAPNTPQYPA
QAGISQQSMA PPYKITHGSM QGSPASANYQ QASMSHSPSG HFVPGQSGPG GRFLPQQGSP
VPSPYAPQSP ATGYRQYPHP PAYSQHQHLQ QGSVASPMIP GAMRNVHENK DQMRMGFTSH
LLQSSPPYTP PCDGTKDLHL GSQDKQRGQK SSEGEQDSPD KATVYDIVGS PAKDHTKLIL
RPSRARPAEV ELGGMYPGSD PEGELVEALA AIERMESEAA METERSAKEV QDKDKPLKKR
KQDSHPQEPG AAGTAGSGSG APGGGGGANA GHRLAPQEAS AAGTSASRPG LQVSLEQAGR
VEDDCMGMPI PASEAQRWPQ EPQEGVTPKA VKHEHDHDPE HPHYDDKQPD TPRQKHRPEG
RHGDGGAQRA AVQSGSKQVE LPPYMLGENT GVLKNFTIPK IRKGELGGGD IPEGWKQPCV
RLERLEADVD VKKSVKPVVV LQKLSIDEVQ RLMRERDSRA SKSGKNRLSS GRSGKGGIDP
SVLKDLPPEL LAEIESTMPL CERVKMNKRK RSTVNERPKY AEDSSEDEEF SSRKRQRKDR
DRTWEAEERD RRSSGEHRRG NFDARRGSGS RYDDSDQDSP PPSLNEVARR LKMKQKKRKV
YEPKLTPEEM MDSSTFKRFT LSIDNILENL EDVDFTAQDD DEIPQELLLG KQQLNELGSE
SAKIKAMGIT SRIPSDKLVK LLNILEKNIL DGASLSTLMN LDNEGEDEER LWRDLIMERV
TKSADACLTA LNIMTSTHMP KAVYIEDVIE RVLQYTKFHL QNTLYPQYDP VYRVNPKGGS
MLSSRAKRAK CSTAKQKVII MLYNKVCDVV SNISELLEIQ LMTDTTILQV SSMGITPFFV
ENVSELQLCA IKLVTAVFSR YEKHRQLILE EIFTSLARLP TSKRSLRNFR LNSSDDEGEP
IYIQMVSALV LQLIQCVVHL PADRDSEDDH KKVDDDVFIT NSYETARRTA QNFLSVFLKK
CGSKQGEEDY RPLFENFVQD LLSTVNKPDW PASELLLSLL GRLLVHQFSN KQTEMALRVA
SLDYLGTVAA RLRKDSVTSR MDQKAIERII RENTEGDETQ RLQKALLDYM DENAETDPAL
AFARKFYIAQ WFRDCTTETE KAMRSQNQKE DDSDGAQHAK ELQATGDIMQ RAETRKKFLH
SVVKSTPNQF TTLRMNSDTV DYDDACLIVR YLASTRPFSQ SFDIYLTQIL RVLGESAIAV
RTKAMKCLSE VVAVDPSILA RSDMQRGVHG RLMDNSTSVR EAAVELLGRF VLSRPQLTEQ
YYDMLIERIL DTGISVRKRV IKILRDICLE QPNFSKITEM CVKMIRRVND EEGIKKLVNE
TFQKLWFTPT PNHDKETMNR KILNITDVVS ACKDTGYDWF EQLLQNLLKS EEDSSYKPTR
KACVQLVDNL VEHILKYEEA LAEHKSVNST RLVACITTLY LFSKIRAQLM VKHAMTMQPY
LTTKCSSQSD FMVICNVAKI LELVVPLMDH PSESFLTTIE EDLMKLILKY GMTVVQYCVS
CLGAIVNKVT HNYKFVWACF NRYYGALTKL KVQHQEGTNS MALAATKAAL LRSLFTAGAL
CRHFDFDLEQ FKGTTKVVIK EKVLELLLYF TNHEDEEVKC KAIIGLGFLF IMHPSQMFVP
EVKTLYNGLL SDKRSSITLK IQVLKNLQMY LQEEDTRMQE ADREWQKLSK QEDLKEMGDI
SSGMSSSIMQ LYLKQVLESF FHAQSSVRHF ALNVIALTLS QGLIHPVQCV PYLIAMGTDA
EPTMRNKADQ QLVEIDKKYT GFIHMKAVAG MKMSYQVQQA VFGSAGSVIR GFRQDESNSA
QCSHLYSMVR ANRQHRRAFL ISLLNLFDDS SKMEVNMLLF IADNLAYFPY QSQEEPLFIM
HHIDITLSVS GSNLLQTFKE SLVKIPGRKS RKRRRRRRRP QRQQPPPPPP QQQQQQNGSE
EERGAQDEER ERHSGDEEYD DDDYEEDEDG HRVRKPKPTE DIRQSESDSD SDLDDVDAVM
ERLPDDSTSL VDFARASQGI LLLLVLKQHL KNLYGFSDGK IQKYSPSESA KVYDKAVNRK
TLANFNPQQT IDFLRHHDVH GELTYELKRK IVKQFLDFKL LMEHLDPDEE DEDGDTSANV
RNKAITALLG GAAASPRNHH TGDSEEDDER SEGEERTPGA SRRGRRTGDS ADLLSANMNE
SVSALDIIAI HCPKYRDRPQ IARVIQKNSD GYSIHWMAGS YSSTWAEAKK RDGRKLVPWV
DSIKETDIIY KKITLTSGNK LNHKVAQTLR SLYAAKDRNS S