RBP10_BOVIN
ID RBP10_BOVIN Reviewed; 620 AA.
AC A3KMV8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Ran-binding protein 10;
DE Short=RanBP10;
GN Name=RANBP10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as an adapter protein to couple membrane receptors to
CC intracellular signaling pathways. Core component of the CTLH E3
CC ubiquitin-protein ligase complex that selectively accepts ubiquitin
CC from UBE2H and mediates ubiquitination and subsequent proteasomal
CC degradation of the transcription factor HBP1. Enhances
CC dihydrotestosterone-induced transactivation activity of AR, as well as
CC dexamethasone-induced transactivation activity of NR3C1, but does not
CC affect estrogen-induced transactivation (By similarity). Acts as a
CC guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an
CC essential role in hemostasis and in maintaining microtubule dynamics
CC with respect to both platelet shape and function (By similarity).
CC {ECO:0000250|UniProtKB:Q6VN19, ECO:0000250|UniProtKB:Q6VN20}.
CC -!- SUBUNIT: May form homodimers. Identified in the CTLH complex that
CC contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or
CC alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within
CC this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8,
CC WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4,
CC MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RAN and
CC RANBP9. Interacts with the HGF receptor MET. Interacts with AR.
CC Interacts with TUBB1. Interacts with YPEL5 (By similarity). May
CC interact with TUBB5. Interacts with DDX4 (By similarity).
CC {ECO:0000250|UniProtKB:Q6VN19, ECO:0000250|UniProtKB:Q6VN20}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6VN20}. Nucleus {ECO:0000250|UniProtKB:Q6VN20}.
CC -!- DOMAIN: The SPRY domain mediates the interaction with MET.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
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DR EMBL; BC133307; AAI33308.1; -; mRNA.
DR RefSeq; NP_001091594.1; NM_001098125.1.
DR AlphaFoldDB; A3KMV8; -.
DR SMR; A3KMV8; -.
DR STRING; 9913.ENSBTAP00000043820; -.
DR PaxDb; A3KMV8; -.
DR GeneID; 519736; -.
DR KEGG; bta:519736; -.
DR CTD; 57610; -.
DR eggNOG; KOG1477; Eukaryota.
DR InParanoid; A3KMV8; -.
DR OrthoDB; 1106989at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR CDD; cd12909; SPRY_RanBP9_10; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035782; SPRY_RanBP9/10.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT CHAIN 2..620
FT /note="Ran-binding protein 10"
FT /id="PRO_0000305236"
FT DOMAIN 35..222
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 253..285
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 291..348
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN19"
SQ SEQUENCE 620 AA; 67249 MW; A5616B6F284709E9 CRC64;
MAAATADPGA GSPQVGDSSG GATGCGLPSP GEQELSRRLQ RLYPAVNQHE TPLPRSWSPK
DKYNYIGLSQ GNLRVHYKGH GKNHKDAASV RATHPIPAAC GIYYFEVKIV SKGRDGYMGI
GLSAQGVNMN RLPGWDKHSY GYHGDDGHSF CSSGTGQPYG PTFTTGDVIG CCVNLINGTC
FYTKNGHSLG IAFTDLPANL YPTVGLQTPG EIVDANFGQQ PFLFDIEDYM REWRAKVQGT
VHCFPISARL GEWQAVLQNM VSSYLVHHGY CATATAFARM TETPIQEEQA SIKNRQKIQK
LVLEGRVGEA IETTQRFYPG LLEHNPNLLF MLKCRQFVEM VNGTDSEVRS LSSRSPKSQD
SYPGSPSLSP RHGPTSSHTH NTGADSPSCS NGVASTKSKQ NHSKYPAPSS SSSSSSSSSS
SSPSSVNYSE SNSTDSTKSQ PHSSTSNQET SDSEMEMEAE HYPNGVLESM STRIVNGAYK
HEDLQTDESS MDDGHPRRQL CGGNQAATER IILFGRELQA LSEQLGREYG KDLAHTEMLQ
DAFSLLAYSD PWSCPVGQQL DPIQREPVCA ALNSAILESQ NLPKQPPLML ALGQASECLR
LMARAGLGSC SFARVDDYLH
