ID A0A452FZ05_CAPHI Unreviewed; 942 AA.
AC A0A452FZ05;
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=Scaffold attachment factor B2 {ECO:0000313|Ensembl:ENSCHIP00000029416.1};
GN Name=SAFB2 {ECO:0000313|Ensembl:ENSCHIP00000029416.1};
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:ENSCHIP00000029416.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000029416.1, 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:ENSCHIP00000029416.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LWLT01000008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017906395.1; XM_018050906.1.
DR AlphaFoldDB; A0A452FZ05; -.
DR STRING; 9925.ENSCHIP00000029416; -.
DR Ensembl; ENSCHIT00000037286.1; ENSCHIP00000029416.1; ENSCHIG00000024547.1.
DR GeneID; 102183590; -.
DR KEGG; chx:102183590; -.
DR CTD; 9667; -.
DR GeneTree; ENSGT00940000161482; -.
DR OMA; VEVRHMP; -.
DR OrthoDB; 5405075at2759; -.
DR Proteomes; UP000291000; Chromosome 7.
DR Bgee; ENSCHIG00000024547; Expressed in thymus and 17 other cell types or tissues.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060008; P:Sertoli cell differentiation; IEA:Ensembl.
DR CDD; cd12679; RRM_SAFB1_SAFB2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034781; SAFB1_2_RBD.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR15683; SCAFFOLD ATTACHMENT FACTOR B-RELATED; 1.
DR PANTHER; PTHR15683:SF4; SCAFFOLD ATTACHMENT FACTOR B2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 30..64
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 406..484
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 106883 MW; 92F62C2CA1612655 CRC64;
MAETLAGSSD SGSATAAVVS GVSEVGTRRL SDLRVIDLRA ELKKRNLDTG GNKSVLMERL
KKAVKEEGQD PDEIGIAFEA TSKKTKRLVK EQKAEEEGTE DNGLEEDSRD GQEDMEASLE
GLQSIDMMDV NVLEETEVEN STAPDFGEDG TDSILESLCE SKDYVATQLR ELPAQFTGHA
VDGEGFENTL DASSLDFKVP PDIEEPLLEP ENEKILDILG ETCKSEPVKE EGSELEQPFA
QETSSVGPDR KLAEEEDLFD SAHPEEGDLD LANESTAHAQ SSKADTLLAV VKREPVEQTG
DDERMDCEPV GLEKPIEQSS KASEHTEACS EEAAEAPPEA SSPDPGDSKE DVKKFAFEAC
NEVPPAPKES SASEGADQKM SSFKEEKDIK PIVKDEKGRI SNSSGRNLWV SGLSSTTRAT
DLKNLFSKYG KVVGAKVVTN ARSPGARCYG FVTMSTSDEA TKCISHLHRT ELHGRMISVE
KAKNEPSGKK LSDRKECEVK KEKLSSVDRH HSVEIKVEKT IIKKEEKMEK KEEKEPEDIK
KEEKDENELK SGPENRSRVT KSGSRGMERT VVMDKSKGEP VISVKTTSRS KERSSKSQDR
KSESKEKRDI LSFDKIKEQR ERERQRQRER EIRETERRRE REQREREQRL EAFHEGKEKA
RLEREREQLD RQWQRLERER LERERLERER ERVERERRRE QERIQREREE LRHQQEQLRY
EQERRSVVRR PYDIGRRDDT GWPEGKRMAM EDRYRPDFPR PDHRFHHFDH RDRGRYQEHG
ADRREGSRSV MGERDGQHYS DERHSHGGPP ERHARDSRDG WGGYGSDKRM SEGRGPPPPP
RGGRDWSEHN QRLEEHQERT WPGTVDADTA GREHSRWQGG ERGLSGPSGP GHMADRGGIS
GRGGFAHGGH TQGDVVPAGG LDSDGLAGQD RGNRDPHFTR HY
//
