BI2L1_RAT
ID BI2L1_RAT Reviewed; 516 AA.
AC Q3KR97; Q5FWT2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1;
DE Short=BAI1-associated protein 2-like protein 1;
GN Name=Baiap2l1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; SER-281; SER-332 AND
RP SER-423, 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: May function as adapter protein. Involved in the formation of
CC clusters of actin bundles. Plays a role in the reorganization of the
CC actin cytoskeleton in response to bacterial infection (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAC1. Binds to F-actin. Interacts with FASLG
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Recruited to actin pedestals that are formed upon infection by
CC bacteria at bacterial attachment sites. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3KR97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3KR97-2; Sequence=VSP_020077;
CC -!- DOMAIN: The IMD domain is predicted to have a helical structure. It may
CC induce actin bundling and filopodia formation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine in response to insulin. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH89216.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC089216; AAH89216.1; ALT_INIT; mRNA.
DR EMBL; BC105815; AAI05816.1; -; mRNA.
DR RefSeq; NP_001029312.1; NM_001034140.1. [Q3KR97-1]
DR AlphaFoldDB; Q3KR97; -.
DR SMR; Q3KR97; -.
DR IntAct; Q3KR97; 2.
DR STRING; 10116.ENSRNOP00000057568; -.
DR iPTMnet; Q3KR97; -.
DR PhosphoSitePlus; Q3KR97; -.
DR PaxDb; Q3KR97; -.
DR PRIDE; Q3KR97; -.
DR GeneID; 304282; -.
DR KEGG; rno:304282; -.
DR CTD; 55971; -.
DR RGD; 1308452; Baiap2l1.
DR VEuPathDB; HostDB:ENSRNOG00000001007; -.
DR eggNOG; ENOG502QQC6; Eukaryota.
DR HOGENOM; CLU_025877_0_1_1; -.
DR InParanoid; Q3KR97; -.
DR OMA; HIHHYHL; -.
DR OrthoDB; 457637at2759; -.
DR PhylomeDB; Q3KR97; -.
DR TreeFam; TF325648; -.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q3KR97; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001007; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q3KR97; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR CDD; cd11913; SH3_BAIAP2L1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR030060; IRTKS.
DR InterPro; IPR035592; IRTKS_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF4; PTHR14206:SF4; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF14604; SH3_9; 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 Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..516
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2-like protein 1"
FT /id="PRO_0000247856"
FT DOMAIN 1..249
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 340..403
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 303..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..516
FT /note="Binds F-actin"
FT /evidence="ECO:0000250"
FT COILED 115..148
FT /evidence="ECO:0000255"
FT COMPBIAS 468..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 413
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020077"
SQ SEQUENCE 516 AA; 57468 MW; 97ED6E2199E853EB CRC64;
MSRGPEEVNR LTENTYRNVV EQFNPGLRNL INLGKNYEKA VNAMILAGKA YYDGVAKIGE
IATGSPVSTE LGHVLIEISS THKKLNETLD ENFKKFHKEI IHELEKKTEL DVKYMNATLK
RYQAEHRNKL DSLEKSQAEL KKIRRKSQGG RNALKYEHKE IEYVETVTSR QSEIQKFIAD
GCKEALLEEK RRFCFLVDKH CSFASHIHRY HLQSAELLNS KLPRWQETCC DATKVPEKIM
NMIEEIKTPI STPVSGTPQP SPMTERSKMI GKDYDTLSKY SPKMPPAPSV KAYTSPLIDM
FNNPATAGQS AEKTNNSTAN TGDDPSLQRS VSVATGLNMM KKQKVKTIFP HTAGNNKTLL
SFAQGDVLTL LIPEEKDGWL YGEHDTTKVR GWFPSSYTKL LEENMKEAMS VPTPSSAPVR
SISTVDLTEK SSVVIPPPDY LECLSMGATS DKRADAAKIP STSTFKAPVP RPDATSTSPS
DSNGTAKPPF LSGENPFATV KLRPTVTNDR SAPIIR
