SRBS2_RAT
ID SRBS2_RAT Reviewed; 1196 AA.
AC O35413; Q923T8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Sorbin and SH3 domain-containing protein 2;
DE AltName: Full=Arg-binding protein 2;
DE Short=ArgBP2;
DE AltName: Full=Arg/Abl-interacting protein 2;
DE AltName: Full=Neural ArgBP2;
DE Short=nArgBP2;
DE AltName: Full=Sorbin;
GN Name=Sorbs2; Synonyms=Argbp2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SAPAP; VCL AND
RP AFDN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10521485; DOI=10.1074/jbc.274.43.30914;
RA Kawabe H., Hata Y., Takeuchi M., Ide N., Mizoguchi A., Takai Y.;
RT "nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that
RT interacts with synapse-associated protein 90/postsynaptic density-95-
RT associated protein (SAPAP).";
RL J. Biol. Chem. 274:30914-30918(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 182-354 (ISOFORM 2), AND AMIDATION AT ALA-148
RP (ISOFORM 2).
RC STRAIN=Wistar;
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 [3]
RP INTERACTION WITH FLOT1; PTK2B AND CBL, AND SUBCELLULAR LOCATION.
RX PubMed=15128873; DOI=10.1242/jcs.01148;
RA Haglund K., Ivankovic-Dikic I., Shimokawa N., Kruh G.D., Dikic I.;
RT "Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for
RT actin reorganization in growing neurites.";
RL J. Cell Sci. 117:2557-2568(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16125169; DOI=10.1016/j.yexcr.2005.06.026;
RA Roenty M., Taivainen A., Moza M., Kruh G.D., Ehler E., Carpen O.;
RT "Involvement of palladin and alpha-actinin in targeting of the Abl/Arg
RT kinase adaptor ArgBP2 to the actin cytoskeleton.";
RL Exp. Cell Res. 310:88-98(2005).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH SYNJ1;
RP SYNJ2; DNM1; DNM2; VCL; WASF; CBL; ABL; SPTAN1 AND PTK2B.
RX PubMed=15659545; DOI=10.1073/pnas.0409376102;
RA Cestra G., Toomre D., Chang S., De Camilli P.;
RT "The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple
RT regulatory mechanisms converging on the actin cytoskeleton.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1731-1736(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-40; SER-143; SER-254;
RP SER-343; SER-354; SER-397; SER-589; SER-645; SER-648; SER-844 AND SER-1113,
RP AND IDENTIFICATION BY 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: 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 (By similarity). May play a role
CC in the regulation of pancreatic cell adhesion, possibly by acting on
CC WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as
CC dephosphorylation by PTPN12 (By similarity). Isoform 2 increases water
CC and sodium absorption in the intestine and gall-bladder. {ECO:0000250,
CC ECO:0000250|UniProtKB:O94875, ECO:0000269|PubMed:10521485}.
CC -!- SUBUNIT: Interacts with ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN, CBL and PALLD
CC (By similarity). Interacts with ABL, CBL, DNM1, DNM2, FLOT1, AFDN,
CC PTK2B/PYK2, SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin and WASF.
CC Interacts with PTPN12 and WASF1 via its SH3 domains; this interaction
CC may mediate the partial PTPN12 and WASF1 translocation to focal
CC adhesion sites. {ECO:0000250, ECO:0000250|UniProtKB:O94875,
CC ECO:0000269|PubMed:10521485, ECO:0000269|PubMed:15128873,
CC ECO:0000269|PubMed:15659545}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10521485, ECO:0000269|PubMed:15128873,
CC ECO:0000269|PubMed:15659545, ECO:0000269|PubMed:16125169}. Apical cell
CC membrane {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35413-1; Sequence=Displayed;
CC Name=2; Synonyms=Sorbin;
CC IsoId=O35413-2; Sequence=VSP_034812, VSP_034813, VSP_034814,
CC VSP_034815;
CC -!- TISSUE SPECIFICITY: Expressed in brain; found in synapses in
CC cerebellum. {ECO:0000269|PubMed:10521485, ECO:0000269|PubMed:15659545}.
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}.
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DR EMBL; AF026505; AAB81527.1; -; mRNA.
DR EMBL; AF396458; AAK81861.1; -; mRNA.
DR PIR; T14108; T14108.
DR RefSeq; NP_446222.1; NM_053770.1.
DR AlphaFoldDB; O35413; -.
DR SMR; O35413; -.
DR BioGRID; 250427; 8.
DR IntAct; O35413; 3.
DR MINT; O35413; -.
DR STRING; 10116.ENSRNOP00000029182; -.
DR iPTMnet; O35413; -.
DR PhosphoSitePlus; O35413; -.
DR PaxDb; O35413; -.
DR PRIDE; O35413; -.
DR GeneID; 114901; -.
DR KEGG; rno:114901; -.
DR CTD; 8470; -.
DR RGD; 620061; Sorbs2.
DR eggNOG; KOG4225; Eukaryota.
DR InParanoid; O35413; -.
DR OrthoDB; 228183at2759; -.
DR PhylomeDB; O35413; -.
DR PRO; PR:O35413; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IGI:BHF-UCL.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR028506; Sorbin_SH3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR14167:SF56; PTHR14167:SF56; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF02208; Sorb; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SMART; SM00459; Sorb; 1.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS50831; SOHO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amidation; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Ubl conjugation.
FT CHAIN 1..1196
FT /note="Sorbin and SH3 domain-containing protein 2"
FT /id="PRO_0000344479"
FT DOMAIN 166..227
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 959..1018
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1034..1095
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1137..1196
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 25..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT VAR_SEQ 1..181
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034812"
FT VAR_SEQ 182..185
FT /note="GIPT -> MISQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034813"
FT VAR_SEQ 326..334
FT /note="VYQSSIDRS -> KPQAGRRKV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034814"
FT VAR_SEQ 335..1196
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034815"
FT CONFLICT 265
FT /note="T -> P (in Ref. 1; AAB81527)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="S -> V (in Ref. 2; AAK81861)"
FT /evidence="ECO:0000305"
FT MOD_RES O35413-2:148
FT /note="Alanine amide"
FT /evidence="ECO:0000269|PubMed:11786189"
SQ SEQUENCE 1196 AA; 134057 MW; 122E5B7B0534B855 CRC64;
MNTDSGGCAR KRAAMSVTLT SVKRVQSSPN LLAAGRESHS PDSAWRSYNG RNPETLNGDA
TYSSLAAKGF RSVRPNLQDK KSPTQSHITI NGNSGGAVSP VSYYQRPFSP SAYSLPASLN
SSIIMPHGRS LDSAETYSQH AQSLDGTMGS SIPLYRSSEE EKRVTVIKAP HYPGIGPVDE
SGIPTAIRTT VDRPKDWYKT MFKQIHMVHK PDEDTDMYNT PYTYNAGLYN SPYSAQSHPA
AKTQTYRPLS KSHSDNGTDA FKEATSPVPP PHVPPRPRDQ SSTEKHDWDP PDRKVDTRKF
RSEPRSIFEY EPGKSSILQH ERPVSVYQSS IDRSLERPSS SASMAGDFRK RRKSEPAVGP
PRGLGDHSSS RTSPGRADLP GSSSTFTTSF ISSSPSSPSR AQGGDDSKMC PPLCSYSGLN
GSPSSELECC GAYRRHLDVP QDSQRAITFK NGWQMARQNA EIWSSTEEAV SPKIKSRSCD
DLLNDDCGSF PDPKTKSESM GSLLCDEGSK ESDPMTWTSP YIPEVCGNSR SRLKHRSAHN
APGFLKMYKK MHRINRKDLM NSEVICSVKS RILQYEKEQQ HRGLLHGWSQ SSTEEVPRDV
VPTRISEFEK LIQKSKSMPN LGDEMLSPVT LEPPQNGLCP KRRFSIESLL EEETQVRHPS
QGQRSCKSNT LVPIHIEVTS DEQPRTHMEF SDSDQDGVVS DHSDNVHVER SSFCSESDFD
HFSFTSSESF YGSSHHHHHH HHHHGHFISS CKGRCPASYT RFTTMLKHER AKHENIDRPR
RQDMDPGLSK LAFLVSPVPF RRKKVLTPQK QTEQAKCKAS VVEALDSALK DICDQIKAEK
RRGSLPDNSI LHRLISELLP QIPKRNSSLN ALKRSPMHQP FHPLPQDGAI HCPLYQNDCG
RMPHSASFPD VDTTSSYHAQ DYGSVLSLQD HESPRSYSST LTDLGRSVSR ERRGTPEKEV
KLPAKAVYDF KAQTSKELSF KKGDTVYILR KIDQNWYEGE HHGRVGIFPI SYVEKLTPPE
KAQPARPPPP VQPGEIGEAI AKYNFNADTN VELSLRKGDR IILLKRVDQN WYEGKIPGTN
RQGIFPVSYV EVVKRNTKGS EDYPDPPLPH SYSSDRIYSL SSNKPQRPVF SHENIQGGGE
PFQALYNYTP RNEDELELRE SDVVDVMEKC DDGWFVGTSR RTKFFGTFPG NYVKRL
