SRBS1_RAT
ID SRBS1_RAT Reviewed; 35 AA.
AC P84109;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Sorbin and SH3 domain-containing protein 1;
DE AltName: Full=Ponsin;
DE AltName: Full=SH3P12;
DE Flags: Fragments;
GN Name=Sorbs1 {ECO:0000250|UniProtKB:Q62417};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver {ECO:0000269|PubMed:10085297};
RX PubMed=10085297; DOI=10.1083/jcb.144.5.1001;
RA Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H.,
RA Mizoguchi A., Takai Y.;
RT "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at
RT cell-cell and cell-matrix adherens junctions.";
RL J. Cell Biol. 144:1001-1017(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in tyrosine phosphorylation of CBL by linking
CC CBL to the insulin receptor. Required for insulin-stimulated glucose
CC transport. Involved in formation of actin stress fibers and focal
CC adhesions (By similarity). {ECO:0000250|UniProtKB:Q62417}.
CC -!- SUBUNIT: Interacts with the long isoform of AFDN and with VCL. AFDN and
CC VCL bind to SORBS1 in a competitive manner and do not form a ternary
CC complex. Interacts with ABL1, CBL, CBLB and INPPL1/SHIP2 through the
CC third SH3 domain. Interaction with ABL1 occurs only after insulin
CC stimulation while this has no effect on the interaction with INPPL1.
CC Interacts with the insulin receptor but dissociates from it following
CC insulin stimulation. Also interacts with SCA7, PTK2/FAK1 and flotillin.
CC Interacts (via SH3 domain 2) with PXN. Interacts (via third SH3 domain)
CC with the Ten-1 ICD form of TENM1; the interaction induces the
CC translocation of SORBS1 to the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:10085297}. Cell membrane
CC {ECO:0000269|PubMed:10085297}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10085297}. Cell junction, focal adhesion
CC {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus matrix {ECO:0000250}.
CC Note=Colocalized with PXN at focal adhesions during myogenic
CC differentiation. Colocalizes with the Ten-1 ICD form of TENM1 in the
CC nucleus (By similarity). Colocalizes with actin stress fibers. Also
CC detected at the plasma membrane and in neuronal intranuclear
CC inclusions. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P84109; -.
DR SMR; P84109; -.
DR STRING; 10116.ENSRNOP00000021289; -.
DR iPTMnet; P84109; -.
DR PaxDb; P84109; -.
DR PRIDE; P84109; -.
DR RGD; 1586598; Sorbs1.
DR eggNOG; KOG4225; Eukaryota.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0030055; C:cell-substrate junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016600; C:flotillin complex; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005899; C:insulin receptor complex; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005158; F:insulin receptor binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:1904608; P:response to monosodium L-glutamate; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Transport.
FT CHAIN <1..>35
FT /note="Sorbin and SH3 domain-containing protein 1"
FT /id="PRO_0000072187"
FT DOMAIN <1..8
FT /note="SoHo"
FT /evidence="ECO:0000250|UniProtKB:Q62417,
FT ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN <22..>35
FT /note="SH3"
FT /evidence="ECO:0000250|UniProtKB:Q62417,
FT ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT NON_CONS 21..22
FT /evidence="ECO:0000303|PubMed:10085297"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:10085297"
FT NON_TER 35
FT /evidence="ECO:0000303|PubMed:10085297"
SQ SEQUENCE 35 AA; 4107 MW; 32D1B32746D48BC3 CRC64;
LNRDDDSDLH SPRYSFSEDT KCDDGWFVGT SRRTK
