BAIP2_CRIGR
ID BAIP2_CRIGR Reviewed; 521 AA.
AC Q60437;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
DE Short=BAI-associated protein 2;
DE Short=BAI1-associated protein 2;
DE AltName: Full=Insulin receptor substrate protein of 53 kDa;
DE Short=IRSp53;
DE Short=Insulin receptor substrate p53;
DE AltName: Full=Insulin receptor tyrosine kinase 53 kDa substrate;
DE AltName: Full=p58/p53;
GN Name=BAIAP2;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-84 AND 264-285, AND
RP PHOSPHORYLATION AT TYROSINE RESIDUES.
RC TISSUE=Ovary;
RX PubMed=8621681; DOI=10.1074/jbc.271.6.3238;
RA Yeh T.C., Ogawa W., Danielsen A.G., Roth R.A.;
RT "Characterization and cloning of a 58/53-kDa substrate of the insulin
RT receptor tyrosine kinase.";
RL J. Biol. Chem. 271:2921-2928(1996).
CC -!- FUNCTION: Adapter protein that links membrane-bound small G-proteins to
CC cytoplasmic effector proteins. Necessary for CDC42-mediated
CC reorganization of the actin cytoskeleton and for RAC1-mediated membrane
CC ruffling. Involved in the regulation of the actin cytoskeleton by WASF
CC family members and the Arp2/3 complex. Plays a role in neurite growth.
CC Acts syngeristically with ENAH to promote filipodia formation. Plays a
CC role in the reorganization of the actin cytoskeleton in response to
CC bacterial infection. Participates in actin bundling when associated
CC with EPS8, promoting filopodial protrusions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been
CC activated by GTP binding. Interacts with ATN1, ADGRB1, DIAPH1, EPS8,
CC SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts with ENAH
CC after recruitment of CDC42 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q60437; Q9NZQ3: NCKIPSD; Xeno; NbExp=3; IntAct=EBI-7010040, EBI-745080;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Detected throughout the cytoplasm in
CC the absence of specific binding partners. Detected in filopodia and
CC close to membrane ruffles. Recruited to actin pedestals that are formed
CC upon infection by bacteria at bacterial attachment sites (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The IMD domain forms a coiled coil. The isolated domain can
CC induce actin bundling and filopodia formation. In the absence of G-
CC proteins intramolecular interaction between the IMD and the SH3 domain
CC gives rise to an auto-inhibited state of the protein. Interaction of
CC the IMD with RAC1 or CDC42 leads to activation (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2,
CC SHANK1, DIAPH1 and ENAH. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by INSR in response to insulin
CC treatment. {ECO:0000269|PubMed:8621681}.
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DR EMBL; U41899; AAC52436.1; -; mRNA.
DR AlphaFoldDB; Q60437; -.
DR SMR; Q60437; -.
DR IntAct; Q60437; 1.
DR MINT; Q60437; -.
DR Ensembl; ENSCGRT00001000832; ENSCGRP00001000808; ENSCGRG00001000617.
DR eggNOG; ENOG502QUM6; Eukaryota.
DR GeneTree; ENSGT00940000153560; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR CDD; cd11915; SH3_Irsp53; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR030128; IRSp53.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR035594; Irsp53_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF3; PTHR14206:SF3; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Phosphoprotein; SH3 domain.
FT CHAIN 1..521
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2"
FT /id="PRO_0000064815"
FT DOMAIN 1..250
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 375..438
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 299..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 132..153
FT /evidence="ECO:0000255"
FT COMPBIAS 323..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKX1"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
SQ SEQUENCE 521 AA; 57639 MW; 58485BD6CAC15DC1 CRC64;
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL
KKYQAEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS
DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPVWQQAC ADPNKIPDRA
VQLMQQIASS NGSILPSTLS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP KNSYATTENK
TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE
KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLAVPPP DYGTSSRAFP
TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSSADVEVAR F
