SRBS2_PIG
ID SRBS2_PIG Reviewed; 158 AA.
AC P28220; Q95ME6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Sorbin and SH3 domain-containing protein 2;
DE AltName: Full=Arg-binding protein 2;
DE Short=ArgBP2;
DE Contains:
DE RecName: Full=Sorbin;
GN Name=SORBS2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Duodenum, and Jejunum;
RX PubMed=11786189; DOI=10.1016/s0196-9781(01)00558-7;
RA Wahbi K., Magaud J.-P., Pansu D., Descroix-Vagne M.;
RT "Coding region of the sorbin gene in different species.";
RL Peptides 22:2045-2053(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-153, AND AMIDATION AT ALA-153.
RC TISSUE=Intestine;
RX PubMed=1915377; DOI=10.1111/j.1432-1033.1991.tb16254.x;
RA Vagne-Descroix M., Pansu D., Joernvall H., Carlquist M., Guignard H.,
RA Jourdan G., Desvigne A., Collinet M., Caillet C., Mutt V.;
RT "Isolation and characterisation of porcine sorbin.";
RL Eur. J. Biochem. 201:53-59(1991).
CC -!- FUNCTION: Adapter protein that plays a role in the assembling of
CC signaling complexes, being a link between ABL kinases and actin
CC cytoskeleton. Can form complex with ABL1 and CBL, thus promoting
CC ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus
CC mediating AKT1-mediated activation of PAK1 (By similarity). May play a
CC role in the regulation of pancreatic cell adhesion, possibly by acting
CC on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as
CC dephosphorylation by PTPN12. Increases water and sodium absorption in
CC the intestine and gall-bladder. {ECO:0000250|UniProtKB:O35413,
CC ECO:0000250|UniProtKB:O94875}.
CC -!- SUBUNIT: Interacts with ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN, AKT1, CBL,
CC PALLD and PAK1 (By similarity). Interacts with ABL, CBL, DNM1, DNM2,
CC FLOT1, AFDN, PTK2B/PYK2, SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin, and
CC WASF. Interacts with PTPN12 and WASF1 via its SH3 domains; this
CC interaction may mediate the partial PTPN12 and WASF1 translocation to
CC focal adhesion sites. {ECO:0000250|UniProtKB:O35413,
CC ECO:0000250|UniProtKB:O94875}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O94875}. Apical cell membrane
CC {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O94875}. Note=Detected in the stress fibers,
CC synaptosomal cytosol, postsynaptic density fraction, Z-disks and
CC intercalated. The CBL/PTK2B/ARGBP2 complex is recruited to lipid rafts
CC following growth factor stimulation. In pancreatic acinar cells,
CC localized preferentially to the apical membrane. Colocalized with
CC vinculin and filamentous actin at focal adhesions and lamellipodia of
CC pancreatic cells. {ECO:0000250|UniProtKB:O94875}.
CC -!- TISSUE SPECIFICITY: Expressed in duodenum.
CC {ECO:0000269|PubMed:11786189}.
CC -!- DOMAIN: The first 2 SH3 domains are required for WASF1-binding. All 3
CC SH3 domains can bind independently to PTPN12.
CC {ECO:0000250|UniProtKB:O94875}.
CC -!- PTM: Ubiquitinated by CBL. {ECO:0000250}.
CC -!- PTM: Dephosphorylated by PTPN12. {ECO:0000250|UniProtKB:O94875}.
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DR EMBL; AF396456; AAK81859.1; -; mRNA.
DR PIR; S17837; S17837.
DR AlphaFoldDB; P28220; -.
DR STRING; 9823.ENSSSCP00000016740; -.
DR PaxDb; P28220; -.
DR PeptideAtlas; P28220; -.
DR PRIDE; P28220; -.
DR eggNOG; KOG4225; Eukaryota.
DR HOGENOM; CLU_1717496_0_0_1; -.
DR InParanoid; P28220; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P28220; SS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR028506; Sorbin_SH3.
DR PANTHER; PTHR14167:SF56; PTHR14167:SF56; 1.
DR Pfam; PF02208; Sorb; 1.
DR SMART; SM00459; Sorb; 1.
DR PROSITE; PS50831; SOHO; 1.
PE 1: Evidence at protein level;
KW Amidation; Cell junction; Cell membrane; Cell projection;
KW Cleavage on pair of basic residues; Cytoplasm; Direct protein sequencing;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..158
FT /note="Sorbin and SH3 domain-containing protein 2"
FT /id="PRO_0000072041"
FT CHAIN 1..153
FT /note="Sorbin"
FT /id="PRO_0000344480"
FT DOMAIN 1..46
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT REGION 28..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 153
FT /note="Alanine amide"
FT /evidence="ECO:0000269|PubMed:1915377"
FT CONFLICT 16
FT /note="W -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="D -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="W -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18180 MW; 00CA1E5F45C60997 CRC64;
MRAATPLQTV DRPKDWYKTM FKQIHMVHKP DDDTDMYNTP YTYNAGLYNS PYSAQSHPAA
KTQTYRPLSK SHSDNGTDAF KDASSPVPPP HVPPPVPPLR PRDRSSTEKH DWDPPDRKVD
TRKFRSEPRS IFEYEPGKSS ILQHERPVTK PQAGRRKV
