Q80Y61 (BI2L2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Baiap2l2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5
Subcellular location	Cell membrane; 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.
Tissue specificity	Expressed in the epithelial layer of the intestine and in the kidney. Ref.5
Domain	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 similarities	Contains 1 IMD (IRSp53/MIM homology) domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing
Ligand	Lipid-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular membrane organization Inferred from direct assay Ref.5. Source: UniProtKB filopodium assembly Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cell-cell contact zone Inferred from sequence or structural similarity. Source: UniProtKB clathrin complex Inferred from electronic annotation. Source: Compara cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell vesicle membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	phospholipid binding Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q80Y61-1)

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.

Isoform 2 (identifier: Q80Y61-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

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

PRO_0000256131

Regions

Domain

1 – 239

239

IMD

Domain

324 – 387

64

SH3

Natural variations

Alternative sequence

205 – 238

34

ARGML…LLGPA → VSRAGESKPRPPGAVVRLRR TQEQERSFLPLCFL in isoform 2.

VSP_021325

Alternative sequence

239 – 522

284

Missing in isoform 2.

VSP_021326

Experimental info

Mutagenesis

109

1

K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-116. Ref.5

Mutagenesis

116

1

K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-109. Ref.5

Mutagenesis

124

1

I → S: Partially impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering. Ref.5

Mutagenesis

127

1

R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-135. Ref.5

Mutagenesis

135

1

K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-127. Ref.5

Mutagenesis

141

1

W → S: Deficient in oligomerization (dimerization maintained). Inefficient formation of planar membrane structures. No effect on lipid-binding. Ref.5

Mutagenesis

145

1

R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-146 and A-147. Ref.5

Mutagenesis

146

1

K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-147. Ref.5

Mutagenesis

147

1

R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-146. Ref.5

Mutagenesis

149

1

K → A: No effect on lipid-binding; when associated with A-152 and A-155. Ref.5

Mutagenesis

152

1

R → A: No effect on lipid-binding; when associated with A-149 and A-155. Ref.5

Mutagenesis

155

1

K → A: No effect on lipid-binding; when associated with A-149 and A-152. Ref.5

Mutagenesis

214

1

L → S: No effect on lipid-binding. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

522

Helix Strand Turn

Details...

Helix

3 – 21

19

Helix

23 – 64

42

Beta strand

65 – 67

3

Helix

69 – 99

31

Helix

101 – 145

45

Helix

151 – 215

65

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 57403388931471FF	FASTA	522	58,402
	10 20 30 40 50 60 MAPEMDQFYR STMAIYKSIM EQFNPALENL VYLGNNYLRA FHALSEAAEV YFSAIQKIGE 70 80 90 100 110 120 QALQSSTSQI LGEILVQMSD TQRHLNSDLE VVVQTFHGDL LQHMEKNTKL DMQFIKDSCQ 130 140 150 160 170 180 HYEIEYRHRA ANLEKCMSEL WRMERKRDKN AREMKESVNR LHAQMQAFVS ESKRAAELEE 190 200 210 220 230 240 KRRYRFLAEK HLLLSNTFLQ FLGRARGMLQ NRVLLWKEQS EASRSPSRAH SPGLLGPALG 250 260 270 280 290 300 PPYPSGRLTP TRLDMPPRPL GEYGSPRSRH GSGSYGPEPA EARSASQLEP DRRSLPRTPS 310 320 330 340 350 360 ASSLYASSTQ RSRSNSFGER LGGGGARRVR ALVSHSEGAN HTLLRFSAGD VVEVLVPEAQ 370 380 390 400 410 420 NGWLYGKLEG SSASGWFPEA YVKPVEEIPV NPMNPVAPMN SMAPMSPMNE LPSRSYPLRG 430 440 450 460 470 480 SHSLDDLLDR PGNPTASSEY WDSQSRSRTP SRVPSRAPSP APPPLPSSRR SSVGSMGAAT 490 500 510 520 DVKKLMSWEQ NPPELFPRGT NPFATVKLRP TVTNDRSAPL IR
	Isoform 2 [UniParc]. Checksum: ED5F84192A0A2227	FASTA	238	27,954
	10 20 30 40 50 60 MAPEMDQFYR STMAIYKSIM EQFNPALENL VYLGNNYLRA FHALSEAAEV YFSAIQKIGE 70 80 90 100 110 120 QALQSSTSQI LGEILVQMSD TQRHLNSDLE VVVQTFHGDL LQHMEKNTKL DMQFIKDSCQ 130 140 150 160 170 180 HYEIEYRHRA ANLEKCMSEL WRMERKRDKN AREMKESVNR LHAQMQAFVS ESKRAAELEE 190 200 210 220 230 KRRYRFLAEK HLLLSNTFLQ FLGRVSRAGE SKPRPPGAVV RLRRTQEQER SFLPLCFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"Pinkbar is an epithelial-specific BAR domain protein that generates planar membrane structures." Pykalainen A., Boczkowska M., Zhao H., Saarikangas J., Rebowski G., Jansen M., Hakanen J., Koskela E.V., Peranen J., Vihinen H., Jokitalo E., Salminen M., Ikonen E., Dominguez R., Lappalainen P. Nat. Struct. Mol. Biol. 18:902-907(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK143783 mRNA. Translation: BAE25539.1.
AL591913 Genomic DNA. No translation available.
CH466550 Genomic DNA. Translation: EDL04661.1.
BC048937 mRNA. Translation: AAH48937.1.

IPI

IPI00228411.
IPI00798612.

RefSeq

NP_808248.1. NM_177580.3.

UniGene

Mm.309647.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OK8	X-ray	2.25	A/B	1-220	[»]

ProteinModelPortal

Q80Y61.

SMR

Q80Y61. Positions 2-220, 323-383.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59098N.

PTM databases

PhosphoSite

Q80Y61.

Proteomic databases

PaxDb

Q80Y61.

PRIDE

Q80Y61.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000165408; ENSMUSP00000127816; ENSMUSG00000018126.
ENSMUST00000170955; ENSMUSP00000125946; ENSMUSG00000018126.

GeneID

207495.

KEGG

mmu:207495.

UCSC

uc007wtb.1. mouse.
uc007wtc.1. mouse.

Organism-specific databases

CTD

80115.

MGI

MGI:2652819. Baiap2l2.

Phylogenomic databases

eggNOG

NOG25242.

GeneTree

ENSGT00390000005995.

HOGENOM

HOG000038005.

HOVERGEN

HBG100621.

InParanoid

Q80Y61.

OMA

TRLDMPP.

OrthoDB

EOG470TH8.

Gene expression databases

ArrayExpress

Q80Y61.

Bgee

Q80Y61.

CleanEx

MM_BAIAP2L2.

Genevestigator

Q80Y61.

GermOnline

ENSMUSG00000018126. Mus musculus.

Family and domain databases

InterPro

IPR013606. IRSp53/MIM_homology_IMD.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF08397. IMD. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

BAIAP2L2. mouse.

NextBio

371953.

SOURCE

Search...

Entry information

Entry name

BI2L2_MOUSE

Accession

Primary (citable) accession number: Q80Y61
Secondary accession number(s): Q3UP58

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program