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Q80Y61

- BI2L2_MOUSE

UniProt

Q80Y61 - BI2L2_MOUSE

Protein

Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2

Gene

Baiap2l2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide.1 Publication

    GO - Molecular functioni

    1. phospholipid binding Source: UniProtKB

    GO - Biological processi

    1. filopodium assembly Source: InterPro
    2. membrane organization Source: UniProtKB
    3. regulation of actin cytoskeleton organization Source: InterPro
    4. signal transduction Source: InterPro

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2
    Short name:
    BAI1-associated protein 2-like protein 2
    Alternative name(s):
    Planar intestinal- and kidney-specific BAR domain protein
    Short name:
    Pinkbar
    Gene namesi
    Name:Baiap2l2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:2652819. Baiap2l2.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Cell junction By similarity. Cytoplasmic vesicle membrane By similarity
    Note: Localizes to RAB13-positive vesicles and to the plasma membrane at intercellular contacts.By similarity

    GO - Cellular componenti

    1. cell-cell contact zone Source: UniProtKB
    2. clathrin complex Source: Ensembl
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell
    5. vesicle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-116. 1 Publication
    Mutagenesisi116 – 1161K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-109. 1 Publication
    Mutagenesisi124 – 1241I → S: Partially impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering. 1 Publication
    Mutagenesisi127 – 1271R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-135. 1 Publication
    Mutagenesisi135 – 1351K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-127. 1 Publication
    Mutagenesisi141 – 1411W → S: Deficient in oligomerization (dimerization maintained). Inefficient formation of planar membrane structures. No effect on lipid-binding. 1 Publication
    Mutagenesisi145 – 1451R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-146 and A-147. 1 Publication
    Mutagenesisi146 – 1461K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-147. 1 Publication
    Mutagenesisi147 – 1471R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-146. 1 Publication
    Mutagenesisi149 – 1491K → A: No effect on lipid-binding; when associated with A-152 and A-155. 1 Publication
    Mutagenesisi152 – 1521R → A: No effect on lipid-binding; when associated with A-149 and A-155. 1 Publication
    Mutagenesisi155 – 1551K → A: No effect on lipid-binding; when associated with A-149 and A-152. 1 Publication
    Mutagenesisi214 – 2141L → S: No effect on lipid-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 522522Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2PRO_0000256131Add
    BLAST

    Proteomic databases

    MaxQBiQ80Y61.
    PaxDbiQ80Y61.
    PRIDEiQ80Y61.

    PTM databases

    PhosphoSiteiQ80Y61.

    Expressioni

    Tissue specificityi

    Expressed in the epithelial layer of the intestine and in the kidney.1 Publication

    Gene expression databases

    BgeeiQ80Y61.
    CleanExiMM_BAIAP2L2.
    GenevestigatoriQ80Y61.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-59098N.

    Structurei

    Secondary structure

    1
    522
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 2119
    Helixi23 – 6442
    Beta strandi65 – 673
    Helixi69 – 9931
    Helixi101 – 14545
    Helixi151 – 21565

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OK8X-ray2.25A/B1-220[»]
    ProteinModelPortaliQ80Y61.
    SMRiQ80Y61. Positions 2-220, 323-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 239239IMDPROSITE-ProRule annotationAdd
    BLAST
    Domaini324 – 38764SH3PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The IMD domain consisting of an antiparallel dimer of three-helix bundles, featuring on one side a positively charged. The N-terminal alpha-helix inserts into the lipid bilayer. Also forms homodimers and homooligomers. The residue Trp-141 is essential for oligomer formation.

    Sequence similaritiesi

    Contains 1 IMD (IRSp53/MIM homology) domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG25242.
    GeneTreeiENSGT00390000005995.
    HOGENOMiHOG000038005.
    HOVERGENiHBG100621.
    InParanoidiQ80Y61.
    OMAiRKRDKNV.
    OrthoDBiEOG7N0C3W.
    PhylomeDBiQ80Y61.
    TreeFamiTF325648.

    Family and domain databases

    InterProiIPR027681. BAIAP2.
    IPR013606. IRSp53/MIM_homology_IMD.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR14206. PTHR14206. 1 hit.
    PfamiPF08397. IMD. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51338. IMD. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q80Y61-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAPEMDQFYR STMAIYKSIM EQFNPALENL VYLGNNYLRA FHALSEAAEV    50
    YFSAIQKIGE QALQSSTSQI LGEILVQMSD TQRHLNSDLE VVVQTFHGDL 100
    LQHMEKNTKL DMQFIKDSCQ HYEIEYRHRA ANLEKCMSEL WRMERKRDKN 150
    AREMKESVNR LHAQMQAFVS ESKRAAELEE KRRYRFLAEK HLLLSNTFLQ 200
    FLGRARGMLQ NRVLLWKEQS EASRSPSRAH SPGLLGPALG PPYPSGRLTP 250
    TRLDMPPRPL GEYGSPRSRH GSGSYGPEPA EARSASQLEP DRRSLPRTPS 300
    ASSLYASSTQ RSRSNSFGER LGGGGARRVR ALVSHSEGAN HTLLRFSAGD 350
    VVEVLVPEAQ NGWLYGKLEG SSASGWFPEA YVKPVEEIPV NPMNPVAPMN 400
    SMAPMSPMNE LPSRSYPLRG SHSLDDLLDR PGNPTASSEY WDSQSRSRTP 450
    SRVPSRAPSP APPPLPSSRR SSVGSMGAAT DVKKLMSWEQ NPPELFPRGT 500
    NPFATVKLRP TVTNDRSAPL IR 522
    Length:522
    Mass (Da):58,402
    Last modified:June 1, 2003 - v1
    Checksum:i57403388931471FF
    GO
    Isoform 2 (identifier: Q80Y61-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         205-238: ARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPA → VSRAGESKPRPPGAVVRLRRTQEQERSFLPLCFL
         239-522: Missing.

    Show »
    Length:238
    Mass (Da):27,954
    Checksum:iED5F84192A0A2227
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei205 – 23834ARGML…LLGPA → VSRAGESKPRPPGAVVRLRR TQEQERSFLPLCFL in isoform 2. 1 PublicationVSP_021325Add
    BLAST
    Alternative sequencei239 – 522284Missing in isoform 2. 1 PublicationVSP_021326Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK143783 mRNA. Translation: BAE25539.1.
    AL591913 Genomic DNA. No translation available.
    CH466550 Genomic DNA. Translation: EDL04661.1.
    BC048937 mRNA. Translation: AAH48937.1.
    CCDSiCCDS37140.1. [Q80Y61-1]
    RefSeqiNP_808248.1. NM_177580.3. [Q80Y61-1]
    UniGeneiMm.309647.

    Genome annotation databases

    EnsembliENSMUST00000165408; ENSMUSP00000127816; ENSMUSG00000018126. [Q80Y61-1]
    ENSMUST00000170955; ENSMUSP00000125946; ENSMUSG00000018126. [Q80Y61-2]
    GeneIDi207495.
    KEGGimmu:207495.
    UCSCiuc007wtb.1. mouse. [Q80Y61-1]
    uc007wtc.1. mouse. [Q80Y61-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK143783 mRNA. Translation: BAE25539.1 .
    AL591913 Genomic DNA. No translation available.
    CH466550 Genomic DNA. Translation: EDL04661.1 .
    BC048937 mRNA. Translation: AAH48937.1 .
    CCDSi CCDS37140.1. [Q80Y61-1 ]
    RefSeqi NP_808248.1. NM_177580.3. [Q80Y61-1 ]
    UniGenei Mm.309647.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OK8 X-ray 2.25 A/B 1-220 [» ]
    ProteinModelPortali Q80Y61.
    SMRi Q80Y61. Positions 2-220, 323-383.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59098N.

    PTM databases

    PhosphoSitei Q80Y61.

    Proteomic databases

    MaxQBi Q80Y61.
    PaxDbi Q80Y61.
    PRIDEi Q80Y61.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000165408 ; ENSMUSP00000127816 ; ENSMUSG00000018126 . [Q80Y61-1 ]
    ENSMUST00000170955 ; ENSMUSP00000125946 ; ENSMUSG00000018126 . [Q80Y61-2 ]
    GeneIDi 207495.
    KEGGi mmu:207495.
    UCSCi uc007wtb.1. mouse. [Q80Y61-1 ]
    uc007wtc.1. mouse. [Q80Y61-2 ]

    Organism-specific databases

    CTDi 80115.
    MGIi MGI:2652819. Baiap2l2.

    Phylogenomic databases

    eggNOGi NOG25242.
    GeneTreei ENSGT00390000005995.
    HOGENOMi HOG000038005.
    HOVERGENi HBG100621.
    InParanoidi Q80Y61.
    OMAi RKRDKNV.
    OrthoDBi EOG7N0C3W.
    PhylomeDBi Q80Y61.
    TreeFami TF325648.

    Miscellaneous databases

    ChiTaRSi BAIAP2L2. mouse.
    NextBioi 371953.
    PROi Q80Y61.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80Y61.
    CleanExi MM_BAIAP2L2.
    Genevestigatori Q80Y61.

    Family and domain databases

    InterProi IPR027681. BAIAP2.
    IPR013606. IRSp53/MIM_homology_IMD.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR14206. PTHR14206. 1 hit.
    Pfami PF08397. IMD. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51338. IMD. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Spleen.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Colon.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-220, FUNCTION, TISSUE SPECIFICITY, PHOSPHOINOSITIDES-BINDING, MUTAGENESIS OF LYS-109; LYS-116; ILE-124; ARG-127; LYS-135; TRP-141; ARG-145; LYS-146; ARG-147; LYS-149; ARG-152; LYS-155 AND LEU-214.

    Entry informationi

    Entry nameiBI2L2_MOUSE
    AccessioniPrimary (citable) accession number: Q80Y61
    Secondary accession number(s): Q3UP58
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3