SH3R1_PONAB
ID SH3R1_PONAB Reviewed; 888 AA.
AC Q5RBR0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. Controls proper
CC cortical neuronal migration and the formation of proximal cytoplasmic
CC dilation in the leading process (PCDLP) in migratory neocortical
CC neurons by regulating the proper localization of activated RAC1 and F-
CC 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 HERP1. Interacts with RAC1; in a GTP-dependent
CC manner. Interacts with MAP3K10/MLK2 and MAP3K11/MLK3. Interacts with
CC MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or
CC SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio. Interacts with
CC SIAH1. Probably part of a signaling complex that may contain SH3RF1,
CC MAPK8IP, DLK1, MAP2K4/MKK4, MAP2K7/MKK7, MAPK8/JNK1, MAPK9/JNK2, AKT1
CC and AKT2. Found in a complex with RAC2, MAP3K7/TAK1, MAP2K7/MKK7,
CC MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2. Found in a complex with RAC1,
CC MAP3K11/MLK3, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1. Interacts with
CC SH3RF2. {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; CR858578; CAH90800.1; -; mRNA.
DR RefSeq; NP_001125455.1; NM_001131983.1.
DR AlphaFoldDB; Q5RBR0; -.
DR SMR; Q5RBR0; -.
DR STRING; 9601.ENSPPYP00000016972; -.
DR GeneID; 100172363; -.
DR KEGG; pon:100172363; -.
DR CTD; 57630; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q5RBR0; -.
DR OrthoDB; 291531at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
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:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
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; PF00018; SH3_1; 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..888
FT /note="E3 ubiquitin-protein ligase SH3RF1"
FT /id="PRO_0000334153"
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 445..506
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 829..888
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 275..321
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 440..543
FT /note="Interaction with AKT2"
FT /evidence="ECO:0000250"
FT REGION 516..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J0"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J0"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZI1"
SQ SEQUENCE 888 AA; 93194 MW; CEA799283F54768E CRC64;
MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV
EELPSNILLV RLLDGIKQRP WKPGPGGGSG TNCTNALRSQ SSTVANCSSK DLQSSQGGQQ
PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVNGIH
GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG
MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGVDAGECS SAAAQSSTAP KHSDTKKNTK
KRHSFTSLTM ANKSSQASQN RHSMEISPPV LISSSNPTAA ARISELSGLS CSAPSQVHIS
TTGLIVTPPP SSPVTTGPSF TFPSDVPYQA TLGTLNPPLL PPPLLAATVL ASTPPGAAAA
AAAAGMGPRP MAGSTDQIAH LRPQTRPSVY VAIYPYTPRK EDELELRKGE MFLVFERCQD
GWFKGTSMHT SKIGVFPGNY VAPVTRAVTN ASQAKVPMST AGQTSRGVTM VSPSTAGGPA
QKLQGNGVAG SPSVVPTAVV SAAHIQTSPQ AKVLLHMTGQ MTVNQARNAV RTVAAHNQER
PTAAVTPIQV QNAAGLSPAS VGLPHHSLAS PQPAPLMPGS ATHTAAISIS RASAPLACAA
AAPLTSSSIT SASLEAEPSG RIVTVLPGLP TSPDSASLAC GNSSATKPDK DSKKEKKGLL
KLLSGASTKR KPRVSPPASP TLEVELGSAE LPLHGAVGPE LPPGGGHGRA GSCPVDGDGP
VTTAVAGAAL AQDAFHRKAS SLDSAVPIAP PPRQACSSLG PVLNESRPVV CERHRVVVSY
PPQSEAELEL KEGDIVFVHK KREDGWFKGT LQRNGKTGLF PGSFVENI
