BI2L2_MOUSE
ID BI2L2_MOUSE Reviewed; 522 AA.
AC Q80Y61; Q3UP58;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2;
DE Short=BAI1-associated protein 2-like protein 2;
DE AltName: Full=Planar intestinal- and kidney-specific BAR domain protein;
DE Short=Pinkbar;
GN Name=Baiap2l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-272; SER-303;
RP SER-472 AND SER-475, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-220, FUNCTION, TISSUE
RP SPECIFICITY, PHOSPHOINOSITIDES-BINDING, AND MUTAGENESIS OF LYS-109;
RP LYS-116; ILE-124; ARG-127; LYS-135; TRP-141; ARG-145; LYS-146; ARG-147;
RP LYS-149; ARG-152; LYS-155 AND LEU-214.
RX PubMed=21743456; DOI=10.1038/nsmb.2079;
RA Pykalainen A., Boczkowska M., Zhao H., Saarikangas J., Rebowski G.,
RA Jansen M., Hakanen J., Koskela E.V., Peranen J., Vihinen H., Jokitalo E.,
RA Salminen M., Ikonen E., Dominguez R., Lappalainen P.;
RT "Pinkbar is an epithelial-specific BAR domain protein that generates planar
RT membrane structures.";
RL Nat. Struct. Mol. Biol. 18:902-907(2011).
CC -!- FUNCTION: Phosphoinositides-binding protein that induces the formation
CC of planar or gently curved membrane structures. Binds to
CC phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate
CC (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a
CC specific phosphoinositide. {ECO:0000269|PubMed:21743456}.
CC -!- INTERACTION:
CC Q80Y61-1; Q80Y61-1: Baiap2l2; NbExp=3; IntAct=EBI-15935597, EBI-15935597;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasmic vesicle
CC membrane {ECO:0000250}. Note=Localizes to RAB13-positive vesicles and
CC to the plasma membrane at intercellular contacts. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80Y61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80Y61-2; Sequence=VSP_021325, VSP_021326;
CC -!- TISSUE SPECIFICITY: Expressed in the epithelial layer of the intestine
CC and in the kidney. {ECO:0000269|PubMed:21743456}.
CC -!- DOMAIN: The IMD domain consisting of an antiparallel dimer of three-
CC helix bundles, featuring on one side a positively charged. The N-
CC terminal alpha-helix inserts into the lipid bilayer. Also forms
CC homodimers and homooligomers. The residue Trp-141 is essential for
CC oligomer formation.
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DR EMBL; AK143783; BAE25539.1; -; mRNA.
DR EMBL; AL591913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL04661.1; -; Genomic_DNA.
DR EMBL; BC048937; AAH48937.1; -; mRNA.
DR CCDS; CCDS37140.1; -. [Q80Y61-1]
DR RefSeq; NP_808248.1; NM_177580.3. [Q80Y61-1]
DR PDB; 3OK8; X-ray; 2.25 A; A/B=1-220.
DR PDBsum; 3OK8; -.
DR AlphaFoldDB; Q80Y61; -.
DR SMR; Q80Y61; -.
DR DIP; DIP-59098N; -.
DR STRING; 10090.ENSMUSP00000127816; -.
DR iPTMnet; Q80Y61; -.
DR PhosphoSitePlus; Q80Y61; -.
DR MaxQB; Q80Y61; -.
DR PaxDb; Q80Y61; -.
DR PeptideAtlas; Q80Y61; -.
DR PRIDE; Q80Y61; -.
DR ProteomicsDB; 265213; -. [Q80Y61-1]
DR ProteomicsDB; 265214; -. [Q80Y61-2]
DR Antibodypedia; 301; 144 antibodies from 25 providers.
DR DNASU; 207495; -.
DR Ensembl; ENSMUST00000165408; ENSMUSP00000127816; ENSMUSG00000018126. [Q80Y61-1]
DR Ensembl; ENSMUST00000170955; ENSMUSP00000125946; ENSMUSG00000018126. [Q80Y61-2]
DR GeneID; 207495; -.
DR KEGG; mmu:207495; -.
DR UCSC; uc007wtb.1; mouse. [Q80Y61-1]
DR UCSC; uc007wtc.1; mouse. [Q80Y61-2]
DR CTD; 80115; -.
DR MGI; MGI:2652819; Baiap2l2.
DR VEuPathDB; HostDB:ENSMUSG00000018126; -.
DR eggNOG; ENOG502QW6V; Eukaryota.
DR GeneTree; ENSGT00940000153560; -.
DR HOGENOM; CLU_025877_1_1_1; -.
DR InParanoid; Q80Y61; -.
DR OMA; MIQTKAP; -.
DR OrthoDB; 457637at2759; -.
DR PhylomeDB; Q80Y61; -.
DR TreeFam; TF325648; -.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 207495; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Baiap2l2; mouse.
DR PRO; PR:Q80Y61; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80Y61; protein.
DR Bgee; ENSMUSG00000018126; Expressed in jejunum and 54 other tissues.
DR GO; GO:0044291; C:cell-cell contact zone; ISS:UniProtKB.
DR GO; GO:0071439; C:clathrin complex; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012506; C:vesicle membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005543; F:phospholipid binding; IDA: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:0061024; P:membrane organization; IDA:UniProtKB.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd11914; SH3_BAIAP2L2; 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; IPR030126; Pinkbar.
DR InterPro; IPR035593; Pinkbar_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF5; PTHR14206:SF5; 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 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Cytoplasmic vesicle; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..522
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2-like protein 2"
FT /id="PRO_0000256131"
FT DOMAIN 1..239
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 324..387
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 220..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 205..238
FT /note="ARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPA -> VSRAGESKPRPPGA
FT VVRLRRTQEQERSFLPLCFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021325"
FT VAR_SEQ 239..522
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021326"
FT MUTAGEN 109
FT /note="K->A: Impairs lipid-binding activity and hence
FT PtdIns(4,5)P2 clustering; when associated with A-116."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 116
FT /note="K->A: Impairs lipid-binding activity and hence
FT PtdIns(4,5)P2 clustering; when associated with A-109."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 124
FT /note="I->S: Partially impairs lipid-binding activity and
FT hence PtdIns(4,5)P2 clustering."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 127
FT /note="R->A: Impairs lipid-binding activity and hence
FT PtdIns(4,5)P2 clustering; when associated with A-135."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 135
FT /note="K->A: Impairs lipid-binding activity and hence
FT PtdIns(4,5)P2 clustering; when associated with A-127."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 141
FT /note="W->S: Deficient in oligomerization (dimerization
FT maintained). Inefficient formation of planar membrane
FT structures. No effect on lipid-binding."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 145
FT /note="R->A: Impairs lipid-binding activity and hence
FT PtdIns(4,5)P2 clustering; when associated with A-146 and A-
FT 147."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 146
FT /note="K->A: Impairs lipid-binding activity and hence
FT PtdIns(4,5)P2 clustering; when associated with A-145 and A-
FT 147."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 147
FT /note="R->A: Impairs lipid-binding activity and hence
FT PtdIns(4,5)P2 clustering; when associated with A-145 and A-
FT 146."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 149
FT /note="K->A: No effect on lipid-binding; when associated
FT with A-152 and A-155."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 152
FT /note="R->A: No effect on lipid-binding; when associated
FT with A-149 and A-155."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 155
FT /note="K->A: No effect on lipid-binding; when associated
FT with A-149 and A-152."
FT /evidence="ECO:0000269|PubMed:21743456"
FT MUTAGEN 214
FT /note="L->S: No effect on lipid-binding."
FT /evidence="ECO:0000269|PubMed:21743456"
FT HELIX 3..21
FT /evidence="ECO:0007829|PDB:3OK8"
FT HELIX 23..64
FT /evidence="ECO:0007829|PDB:3OK8"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3OK8"
FT HELIX 69..99
FT /evidence="ECO:0007829|PDB:3OK8"
FT HELIX 101..145
FT /evidence="ECO:0007829|PDB:3OK8"
FT HELIX 151..215
FT /evidence="ECO:0007829|PDB:3OK8"
SQ SEQUENCE 522 AA; 58402 MW; 57403388931471FF CRC64;
MAPEMDQFYR STMAIYKSIM EQFNPALENL VYLGNNYLRA FHALSEAAEV YFSAIQKIGE
QALQSSTSQI LGEILVQMSD TQRHLNSDLE VVVQTFHGDL LQHMEKNTKL DMQFIKDSCQ
HYEIEYRHRA ANLEKCMSEL WRMERKRDKN AREMKESVNR LHAQMQAFVS ESKRAAELEE
KRRYRFLAEK HLLLSNTFLQ FLGRARGMLQ NRVLLWKEQS EASRSPSRAH SPGLLGPALG
PPYPSGRLTP TRLDMPPRPL GEYGSPRSRH GSGSYGPEPA EARSASQLEP DRRSLPRTPS
ASSLYASSTQ RSRSNSFGER LGGGGARRVR ALVSHSEGAN HTLLRFSAGD VVEVLVPEAQ
NGWLYGKLEG SSASGWFPEA YVKPVEEIPV NPMNPVAPMN SMAPMSPMNE LPSRSYPLRG
SHSLDDLLDR PGNPTASSEY WDSQSRSRTP SRVPSRAPSP APPPLPSSRR SSVGSMGAAT
DVKKLMSWEQ NPPELFPRGT NPFATVKLRP TVTNDRSAPL IR
