ID G3PXA1_GASAC Unreviewed; 2608 AA.
AC G3PXA1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Nipped-B protein {ECO:0000256|RuleBase:RU364107};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000022240.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000022240.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000022240.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364107}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family.
CC {ECO:0000256|ARBA:ARBA00009252, ECO:0000256|RuleBase:RU364107}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 69293.ENSGACP00000022240; -.
DR Ensembl; ENSGACT00000022282.1; ENSGACP00000022240.1; ENSGACG00000016835.1.
DR eggNOG; KOG1020; Eukaryota.
DR GeneTree; ENSGT00390000010427; -.
DR InParanoid; G3PXA1; -.
DR OMA; LYIQMVS; -.
DR TreeFam; TF313121; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000016835; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0009790; P:embryo development; IEA:UniProt.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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:SF18; NIPPED-B-LIKE PROTEIN; 1.
DR PANTHER; PTHR21704; NIPPED-B-LIKE PROTEIN DELANGIN SCC2-RELATED; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU364107};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364107};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU364107}.
FT DOMAIN 2097..2277
FT /note="Sister chromatid cohesion C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12830"
FT REGION 128..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2292..2318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2471..2504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2471..2485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2608 AA; 294674 MW; E4063A06CEF414ED CRC64;
MNGDMPHVPI TTLAGIASLT DLLNQLPLPS PLPATTAKSL LYNGRISEEV SNLLVCRDEN
LVTQLAHSLN QVSTEHIELK DNLGNDEPEG DMPMLLQTLL SLNPKIFRDK SMPSVMQQPM
LQQYKLSQNQ VHGSPGSNYQ QTSVPQSPSG CFASPQSGSS ARFLPQQNSP IPSPYTPQSP
ADYMQYNPPS YSQHQQTQQG QNGVTNPLTS SFRNIHDDKV SGQLSSTSSN HNARLGSDED
YINMAHRLGD EENDPSMRAA TFPVKSPESL CSPAGSEEAA KTGSRPPLIM QSPPPDMPPV
AAPDLHLTSA DRKKKQKERS KEENELTDKN ASYGIVSSPA KESARLTIKL SRVKLADSDQ
SGELPQRPLL DSEHETDLTN NSNTPMSRTA QDPSHRFVAE EQANCKPVPV RPNSKESGVV
SGVVFDDAEI DTLAEIERIE RESASEKERW SKEVQDKDKP LKKRKQDTYP QEPGGDSGDG
PTVQGGNTDS KLRSKKTNAA SNGASRPALM VSIDLQQAGR IKGQPVVVLE AQTFCEDHLR
HLKTKPDGKV DKVAANRPGI IKQNADNPRK SCSDRQPEAL KQKPESQRES KHKHEGKTGS
GKKHSEDRRL DTPRPKHDKH SEQRSKEEKN HNIHRPHISN PETPKTASKA ERNSKHGDGK
DDKDKDKIGD KNREKVRDRE GDKEKQEKNK TRDRDKDRKH KTSRENCSRP SPDRPTKPDS
PRVKQDDGGK STDLNGRQKT ESSGLQNAQN KKDRKSGDGS ASCQAGNNKQ QPLETKHCEF
PSYLLGGKSG SLKNFVIPKL KRDVKDLQLP DKLIESWTEP LVRLERLSLI KDLNKGTKPV
VVLNKLNLDE VKRIIKESRN TNSTRFLDKS GRDMHAKLLC IDNSPKSIDY SVLNTNFLPE
NKRKHSVVSK KSKYAELEED SDDSDDNDDG DNSDNESPKK RYKKDHDKSW KHEERKGTGQ
HRSGGSHGAR RGSGSGHREK SPDGSDQDSP APSLRDIARK LKKKEKQKTK KAYDSKLTPE
EKLDSSTFKR FTANMDSIIE SLEDVDLTAA ADDDEIPEEL LLGKHQLNEL GNDSAKIKAM
CIFNKCSTKK LVKMLNILEK NIQDSVKLST LMNHENDSMD EERLWRDLIM ERVAKSADAC
LTALNIMTSP HMPKAVYIED VIERVLQYTK FHLQNSLYPQ YDPVYRKGQH SCGMHTSKSK
RAKISTHKQK VVVMLYDKVC DIVSNISELL EIQLLTDTTI LQVSTLGITP FFVENVSELQ
LCAITLVTAV FSRYEKHRQL ILEEIFTSLA RLPTSKRSLR NFRLNNDSDE EPLHIQMVTA
LVLQLIQCVV RLPSERDAEG EHNKKVDKDV FITNSYETAM RTAQNFLSVF LKKCGSKQGE
DDYRPLFENF VHDLLSAVNR PEWPAAELLL SLLGRLLVHQ FSNKHTEMAL RVASLDYLGT
VASSLRKDAV NSNVDQKAID RILRETQGSD EIPKLQKALL DYIHEHMETD PALVFARKFY
IAQWFRDTIT EADKAVKSQN DDEDLRHQSM DVDSTEEIVQ RAETRKKFLR KVMKTSPSDW
SSFSINSDTV AYEDSCLIVR YLASMRPFSQ SFDIYLSQIL RVLGESAIAV RTKAMKCLSE
VVAVDPSILA RLDMQRGVHC RLMDNSTSVR EAAVELLGRF VLSRPQLIEQ YYDMLIERIL
DTGISVRKRV IKILRDICLE LPDFHKITEM CVRMIRRVND EEGIKKLVNE TFQKIWFTPT
PSHDKNAMTR KILNITDVVS ACKDTGYDWF EQLLQNLLKS EEQASYKPAK KACVQLVDNL
VEHILKSEES IADCEDKGVI SGRLVACITT LYLFTKIRAQ LMVKHAMTLQ PYLTTKCNTQ
NDFVVICNVA KILELVVPLM EQPSENFLTT IEEDLMKLII KYGMTVVQHS VSCLGAVVNK
VTHNYKFVWA CFNRYYGALA KLKTQHQEDA NSLTLAANKP TLLRALFTVG ALCRHFDFDQ
EEFKGANKIV IKDKVLELLL YFTTHEDEEV QIKALTGLGF QFIMHPEVMF VQDVKVLYNN
TLSDETSLVT LKIQVLKNLQ TYLSEEDSRM QVADREWKNQ AKQEDLKEMG DISSGMSSSI
MQIYLKQVLE SFFHSQSTVR HFALSVIILT LSQGLVHPVQ CVPYLIAMGT DPEPTMKNKA
DQQLAEIDKK YCGFIHMKAV AGLKMSYQVQ QAINGSKGAV IRGFRHDDSD SSLCSHLYTL
VRGNRQHRRA FLISLLNLFD DSSKTEVNRL LFIADNLAYF PYQTQEEPLF IMHHVDITLS
VSGSNLLQSF KESLQKGSEE EDNEQSSSTS SSSDEEEEEV VHSQKKLALF DSDGDEDEDA
VMDRLPENPN PLLDFASASQ GILLLLVLKQ HLKNLYGFSD SKIQKYSPTE SAKVYDKAVN
RKSKVHFNPR QTLEYLKRDL DNADLSIEIK RNIVKQYLDF KVLMEHLDRD EEDEEGEASA
NARNKAITAL LKVPKSSNQN HTKNEPVPVE TDEEESEEEE APVTGHMNER VKAMDIIAIW
CPKYKDRPQI ARVIQRIKTG YSIHWMTGSY SGSWTEVKKR EGRKKVPWVD NIKESDIIYK
KISLSSGHKL TNKVAETLRA LYAAKDGD
//
