ID A0A452EDG3_CAPHI Unreviewed; 3017 AA.
AC A0A452EDG3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=RAN binding protein 2 {ECO:0000313|Ensembl:ENSCHIP00000010201.1};
GN Name=RANBP2 {ECO:0000313|Ensembl:ENSCHIP00000010201.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000010201.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000010201.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000010201.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; LWLT01000009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000017974.1; ENSCHIP00000010201.1; ENSCHIG00000012686.1.
DR GeneTree; ENSGT00940000154389; -.
DR Proteomes; UP000291000; Chromosome 11.
DR Bgee; ENSCHIG00000012686; Expressed in thymus and 17 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR CDD; cd14684; RanBD1_RanBP2-like; 1.
DR CDD; cd13177; RanBD2_RanBP2-like; 1.
DR CDD; cd14685; RanBD3_RanBP2-like; 1.
DR CDD; cd13178; RanBD4_RanBP2-like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 4.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR022011; IR1-M.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23138:SF169; E3 SUMO-PROTEIN LIGASE RANBP2; 1.
DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
DR Pfam; PF12185; IR1-M; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00638; Ran_BP1; 4.
DR Pfam; PF00641; zf-RanBP; 5.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 1.
DR SMART; SM00547; ZnF_RBZ; 5.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 3.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 4.
DR PROSITE; PS50199; ZF_RANBP2_2; 4.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT REPEAT 60..93
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1159..1295
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1339..1369
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1401..1430
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1460..1489
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1579..1608
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1812..1948
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2109..2245
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2707..2842
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2860..3016
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 760..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2074..2112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2277..2305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2356..2427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2601..2635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2379..2413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3017 AA; 334839 MW; 10221E406653A8B3 CRC64;
MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS TYINVQERDP
KAHRFLGLLY EVEENIEKAV ECYKRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL FDLIQSELYA RPDDVHVNIR LVELYRSNSR
LRDAVAHCHQ AERNTALRSS LEWNSCVVQT LKEYLESSQC LESDKSNWRA TSQDLLIAYA
NLMLLTLSIR DAQESRELLE SFDSTLQSVK SCSGGNEELS ATFLEVRGHF YMHAGSLLLK
MGQHSDVQWR ALSELAALCY LIAFQVPRPK TKLIKGEAGQ SLLEMMAYDR LSQSGHMLVN
LSRDKQDFLK EVVESFANRS GQSALYDALF SRQLPKDSSF LGSDDIGSID VQEPDPDELA
RYDVGAIRAH NGSLQHLTWL GLQWDSLPTL PAIRKWLKQL FHHLPQETSR LETNAPESIC
ILDLEVFLLG VIYTSHLQLK EKSNSHCSFY QPLCLPLPVC KQLCTERQKA WWDAVCNLIH
RKAVPGTSAK LRLLVQRDIN TLRGQEKTGL QPALLVHWAK CLQKTGSGLN SFYDQREYIG
RSVHYWKKVL PLLKMIKKKS SIPEPADPLF RHFHSADIQA CEVGEYEDEA HITFAILDVV
NGNIDDAMAT FESINNVTSY WNLALLFHRK AEDIDNDVLS SEEQEECKNY LRKTRDYLIK
ILDDCDSNLS VVKKLPVPLE SVKEMLNLVM QELDEFSEGA PLHKNGSLRN ADSEIKHSTS
SPTKYSPSPN RSCKYSPKTP PQWAEDQNCL LKMICQQVEA IKKEMQELKL NSSSSGSPHR
WPPENYGPDP VPDSYQGSQN FHGAPLTVAT TGHSVCYSQS PAYNTQYLLR PAANVTPTKG
PVYGMNRLPP QQHVYGYPQQ MHTPPVQSSS ACMFSQDMYG PPLRFESPAT GILSPRGDDY
FNYNVQQTST NPPLPEPGYF TKPPLAAHAS RSAEPKVLEF GKTSFVQPVP GEGMRPSLAA
PAHTTQPTPF KFNSNFKSND GDFTFSSPQV VAQPPAATYN NNESLLGLLT SDKPLQGDGY
SGPKAVQNMG PRNTFNFGSK NNMSTNQPKN SGFRRNDDMF TFYSPGKSVF GVPATESASK
GHDADGGSAQ GDEEDDGPHF EPVVPLPDKI EVRTGEEDEE EFFCNRAKLY RFDAASREWK
ERGIGNVKIL RHKTSGKIRL LMRREQVLKI CANHYISPDM ALAPNAGSDR SFVWYAVDYA
DESPKPEQLA IRFKTPEEAA LFKCKFEEAQ SLLKASGGNI ATTTHQATKT VKEPTGHDSK
DIDKSDGVTM NFEFQVAKKE GSWWHCNICS LKNMATAKKC VSCQNLNPGS KELLGPPLVD
TVSAPKPGSD PSRSALVTLK KEGHWNCGVC LVRNEPTVSR CIACQNKNES PLIKQPSFKF
GQGDLPKAAS SDFKSVFSVK EGQWDCSVCL IGNEGSSVKC EACQTPRKQS SPAFAAPAPA
SLKFGTSETS KAPKSGFEGV FSKKEGQWDC SVQNEASMAE CVACQNSGQN PPASAASASA
SSETGKAPKS GLEGLFAKKE GQWDCDVCLI RNEGSSPKCV ACGASNPTQN PAAEAPLTFP
VGSAADASNS CASQTGTGFK SNFSEKAFKF GNAEQGFKFG HVDQENAPSF KFQSSSSTDS
KSAKEGFSFS FPASAGGFKF GIQETENQEK TAEKSFEEDT DDQAQDTGGQ KDGNTVVFGQ
TGSTFTFADL AKSNSGEGFQ FGKKDPNFKG FSGAGEKLFS SQSSKLVDKA DACADLEKDD
DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV KLFRFDAEIS QWKERGLGNL
KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMHLKPLSG SDRAWMWLAS DFSDGDAKLE
QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP LQTPHKLVDT GRAAKLIQRA EEMKSGLKDF
KTFLTNDQTK VSDEESKDSR AGAATAADMS GAPNTETTGP TLEWDNYDLR EDALDDSVSS
SSVHASPLAS SPVRKNLFRF GESTTGFNFS FKSALSPSKS PGKLNQSGAS VGTDEDSDVT
QEEERDGQHF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY RYDKDAGQWK ERGIGDIKIL
QNYENKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER VWVWTACDFA DGERKIEHLA
VRFKLQDVAD SFKKIFDEAK VAQEKDFLIT PHVARSTTPR ESPCGKMAVA VLEETTRERT
DLPQGGDAAD TASEVGGVSG TPETATKAVV SPPKFVFGSE SVKSIFSSEK SKPFAFGNSS
ATGSLFGFSF NTPLKNNSSE ASSAVQSGSE RKVEPSGRQE SQNSDPKSAS DGKVKNTSSA
FLKEQFSTSQ TFKTPEKVEE REKPEDLPSD DDVLIVYELT PTPEQRALAS RLQLPPTFFC
YKNRPDYISE EEEDDEDFDT AVKKLNGKLY LDDSETCRLS EENLTDNEKE CVIVWEKKPT
VEEKAKADTL KLPPTFFCGV CSDTDEDNGN AEDFQSELQK VQEAQKSQEE NIGSSADGMC
TDDTKVTAPF FCKSEEPEFT TKSVSSPSVS SGAVDKPVDL STRKENDADS TSQVESKTVT
FGFGSGTGLS FADLASSNSG DFAFGSKDKN FQWANTGAAV FGAQSTGKVG EDEDGSDEEV
VHNEDIHFEP IVSLPEVEVK SGEEDEEILF KERAKLYRWD REASQWKERG VGDMKILWHT
VKNYFRILMR RDQVFKVCAN HVITKTMELK PLNVSNNALV WTASDYADGE AKVEQLAVRF
KTKEMADCFK KKFEECQQNL LKPQKSLTAE FSNETNPVVF FDICADDEPL GRITMELFSN
IVPKTAENFR ALCTGEKGFG FKSSIFHRVI PDFVCQGGDI TKHDGTGGRS IYGDKFEDEN
FNVKHTGPGL LSMANRGQDT NNSQFFITLK KAERLDFKHV VFGFVKDGMD TVKKIESFGS
PKGSVSRRII ITECGQI
//
