SH3R1_BOVIN
ID SH3R1_BOVIN Reviewed; 840 AA.
AC A5D7F8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q7Z6J0};
DE AltName: Full=Plenty of SH3s;
DE Short=Protein POSH;
DE AltName: Full=RING-type E3 ubiquitin transferase SH3RF1 {ECO:0000305};
DE AltName: Full=SH3 domain-containing RING finger protein 1;
GN Name=SH3RF1; Synonyms=POSH, POSH1 {ECO:0000250|UniProtKB:Q7Z6J0};
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=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of
CC an external substrate, it can catalyze self-ubiquitination. Stimulates
CC ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-
CC dependent and clathrin-independent endocytosis. Acts as a scaffold
CC protein that coordinates with MAPK8IP1/JIP1 in organizing different
CC components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or
CC MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a
CC functional multiprotein complex to ensure the effective activation of
CC the JNK signaling pathway. Regulates the differentiation of CD4(+) and
CC CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation.
CC Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells
CC and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial
CC role in the migration of neocortical neurons in the developing brain.
CC Controls proper cortical neuronal migration and the formation of
CC proximal cytoplasmic dilation in the leading process (PCDLP) in
CC migratory neocortical neurons by regulating the proper localization of
CC activated RAC1 and F-actin assembly. {ECO:0000250|UniProtKB:Q69ZI1,
CC ECO:0000250|UniProtKB:Q7Z6J0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q7Z6J0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RAC1; in a GTP-dependent manner. Interacts with
CC MAP3K10/MLK2 and MAP3K11/MLK3. Interacts with MAPK8IP; this interaction
CC leads to the PJAC complex (POSH-JIP or SH3RF1/MAPK8IP apoptotic
CC complex) with a 1:1 ratio. Interacts with SIAH1. Interacts with HERP1.
CC Probably part of a signaling complex that may contain SH3RF1, MAPK8IP,
CC DLK1, MAP2K4/MKK4, MAP2K7/MKK7, MAPK8/JNK1, MAPK9/JNK2, AKT1 and AKT2.
CC Found in a complex with RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1,
CC MAPK8/JNK1 and MAPK9/JNK2. Found in a complex with RAC1, MAP3K11/MLK3,
CC MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1. Interacts with SH3RF2.
CC {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q71F54,
CC ECO:0000250|UniProtKB:Q7Z6J0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in
CC lamellipodia. Colocalizes, with HERP1, in trans-Golgi network.
CC {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
CC -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC activity and autoubiquitination. {ECO:0000250|UniProtKB:Q7Z6J0}.
CC -!- PTM: Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated,
CC it has reduced ability to bind Rac. {ECO:0000250|UniProtKB:Q7Z6J0}.
CC -!- PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-
CC mediated degradation. {ECO:0000250|UniProtKB:Q71F54}.
CC -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
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DR EMBL; BC140539; AAI40540.1; -; mRNA.
DR RefSeq; NP_001091534.1; NM_001098065.1.
DR AlphaFoldDB; A5D7F8; -.
DR SMR; A5D7F8; -.
DR STRING; 9913.ENSBTAP00000001976; -.
DR PaxDb; A5D7F8; -.
DR PRIDE; A5D7F8; -.
DR Ensembl; ENSBTAT00000001976; ENSBTAP00000001976; ENSBTAG00000001508.
DR GeneID; 528315; -.
DR KEGG; bta:528315; -.
DR CTD; 57630; -.
DR VEuPathDB; HostDB:ENSBTAG00000001508; -.
DR VGNC; VGNC:34579; SH3RF1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155875; -.
DR HOGENOM; CLU_015769_1_0_1; -.
DR InParanoid; A5D7F8; -.
DR OMA; LVCERYR; -.
DR OrthoDB; 291531at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000001508; Expressed in ruminant reticulum and 102 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0043370; P:regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
DR CDD; cd11930; SH3_SH3RF1_2; 1.
DR CDD; cd11785; SH3_SH3RF_C; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR InterPro; IPR035795; SH3RF1_SH3_2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 3.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF50044; SSF50044; 4.
DR PROSITE; PS50002; SH3; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Golgi apparatus; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..840
FT /note="E3 ubiquitin-protein ligase SH3RF1"
FT /id="PRO_0000334150"
FT DOMAIN 134..193
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 196..259
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 439..500
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 781..840
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 12..53
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 105..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..362
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J0"
FT REGION 394..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..537
FT /note="Interaction with AKT2"
FT /evidence="ECO:0000250"
FT REGION 516..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J0"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZI1"
SQ SEQUENCE 840 AA; 87592 MW; 3455AB763557285D CRC64;
MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV
EQLPSNILLV RLLDGIKQRP WKPGPVGGSG TNGTSALRAQ SSAVVTCSPK DGPSSQGGPQ
PRAQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IVLRRQVDEN WYHGEVGGVH
GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG
MLADKIGIFP ISYVEFNSAA KQLIEWDQPP GPGVAAGEGA LATTPSSTTT KQPDGKKNTK
KRHSFTSLSM ASKASQAAQQ RHSMEISPPV LISSSNPAAA ARIGELAGLS CSAPSQVHIS
TTGLIVTPPP SSPVTTGPSF TFPAEAPYPA ALATLNPPLP PPPLQAATPT GTAVAAAAGM
GPRPTAGPTD QTTHPRPQPR PSVYVAIYPY TPRKEDELEL RKGEMFLVFE RCQDGWFKGT
SMHTSKIGVF PGNYVAPVTR AVTSASQGKV PMLTTGPASR GGVLANPPST GGPAQKPPGN
GVAGGPGVPT AVVSAAHVQT SPQAKVLLHA SGQMTVNQAR SAARTVSAHS QERPTAAVTP
IQVQSTPGQS HHPLVSPQPP APLGPPAHAA ASGLGRVGGP LACATAPASI PAASLEPEPS
SRPATLLPGT PTSPDSGSAA RPDKDGKKEK KGLLKLLSGA STKRKPRGSP PASPTLDAEL
GAELSCGPPG PPCACPGPCD GDTMAPGPQR RASSLDSAPV APPPRQPCSS LGPAASEVRP
AVCERHRVVV SYPPQSEAEL ELKEGDIVFV HKKREDGWFK GTLQRNGKTG LFPGSFVENI
