ID A0A7L0LD51_9SYLV Unreviewed; 423 AA.
AC A0A7L0LD51;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=Proline-serine-threonine phosphatase-interacting protein 1 {ECO:0000256|ARBA:ARBA00071018};
DE Flags: Fragment;
GN Name=Pstpip1 {ECO:0000313|EMBL:NXK66757.1};
GN ORFNames=SYLVIR_R00903 {ECO:0000313|EMBL:NXK66757.1};
OS Sylvietta virens (Green crombec).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Acrocephalinae; Sylvietta.
OX NCBI_TaxID=208069 {ECO:0000313|EMBL:NXK66757.1, ECO:0000313|Proteomes:UP000567822};
RN [1] {ECO:0000313|EMBL:NXK66757.1, ECO:0000313|Proteomes:UP000567822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-009-59 {ECO:0000313|EMBL:NXK66757.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXK66757.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in regulation of the actin cytoskeleton. May
CC regulate WAS actin-bundling activity. Bridges the interaction between
CC ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a
CC scaffold protein between PTPN12 and WAS and allow PTPN12 to
CC dephosphorylate WAS. Has the potential to physically couple CD2 and
CC CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-
CC cell:APC contact site so as to promote the actin polymerization
CC required for synapse induction during T-cell activation. Down-regulates
CC CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has
CC a role in innate immunity and the inflammatory response. Recruited to
CC inflammasomes by MEFV. Induces formation of pyroptosomes, large
CC supramolecular structures composed of oligomerized PYCARD dimers which
CC form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to
CC bind to PYCARD and facilitates pyroptosome formation. Regulates
CC endocytosis and cell migration in neutrophils.
CC {ECO:0000256|ARBA:ARBA00057396}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell
CC projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell
CC projection, uropodium {ECO:0000256|ARBA:ARBA00060447}. Cleavage furrow
CC {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXK66757.1}.
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DR EMBL; VXAN01000296; NXK66757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0LD51; -.
DR Proteomes; UP000567822; Unassembled WGS sequence.
DR GO; GO:0005884; C:actin filament; IEA:TreeGrafter.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR GO; GO:0030041; P:actin filament polymerization; IEA:TreeGrafter.
DR CDD; cd11824; SH3_PSTPIP1; 1.
DR FunFam; 1.20.1270.60:FF:000037; Proline-serine-threonine phosphatase interacting protein 1; 1.
DR FunFam; 2.30.30.40:FF:000150; Proline-serine-threonine phosphatase interacting protein 1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030777; PSTPIP1_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF51; PROLINE-SERINE-THREONINE PHOSPHATASE-INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000567822};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..260
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 366..423
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 119..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXK66757.1"
FT NON_TER 423
FT /evidence="ECO:0000313|EMBL:NXK66757.1"
SQ SEQUENCE 423 AA; 48566 MW; 6BABC534E7ABD252 CRC64;
ITFSFCLQCK EFTFHTGYEV LVQRLLEGKK MCKDVEDLLK QRAQAEERYG KELVQIARKA
GGQTEINTLK AAFEMLKQQI ESVGNSHIQL AVMLKEELKG IEEFRERQKE QRKKYESAME
RMQKSKLSHY KKTMESKKTY EQKCREADEA EQSLERTSAS GNQKQTEKSQ NRARQCRDAA
HEAENMYKQN IEQLDKVRTE WEQEHIKTCE VFQLQECDRI TILRNSLWVH CNQLSLQCVK
DDELYEEVRV SLENCVVESD IDYFIKTKMT GTQPPDAIGY ENYYSREPNR CSSSPTQSCG
MLKRFSGLLH GSSKNNTESA TPSAPPLATE LFVSLVGISA LFPPSLTERT DGVYASIFVN
EKAGITSSQD YRVLYDYTAQ NVDELDISEG DTVVVIAENE DGWWTAERNG QRGFVPGSYL
EKL
//
