BI2L2_HUMAN
ID BI2L2_HUMAN Reviewed; 529 AA.
AC Q6UXY1; B0QYE2; Q96BG7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
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; ORFNames=UNQ9336/PRO34007;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21743456};
CC Peripheral membrane protein {ECO:0000269|PubMed:21743456}. Cell
CC junction {ECO:0000269|PubMed:21743456}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:21743456}. Note=Localizes to RAB13-positive
CC vesicles and to the plasma membrane at intercellular contacts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6UXY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UXY1-2; Sequence=VSP_021324;
CC -!- TISSUE SPECIFICITY: Expressed in the epithelial layer of the intestine
CC (at protein level). {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 (By similarity). {ECO:0000250}.
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DR EMBL; AY358164; AAQ88531.1; -; mRNA.
DR EMBL; AL022322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015619; AAH15619.1; -; mRNA.
DR CCDS; CCDS43018.1; -. [Q6UXY1-1]
DR RefSeq; NP_079321.3; NM_025045.5. [Q6UXY1-1]
DR RefSeq; XP_005261808.1; XM_005261751.4. [Q6UXY1-1]
DR RefSeq; XP_011528681.1; XM_011530379.2. [Q6UXY1-2]
DR AlphaFoldDB; Q6UXY1; -.
DR SMR; Q6UXY1; -.
DR BioGRID; 123120; 6.
DR IntAct; Q6UXY1; 1.
DR STRING; 9606.ENSP00000371085; -.
DR iPTMnet; Q6UXY1; -.
DR PhosphoSitePlus; Q6UXY1; -.
DR BioMuta; BAIAP2L2; -.
DR DMDM; 74749434; -.
DR jPOST; Q6UXY1; -.
DR MassIVE; Q6UXY1; -.
DR PaxDb; Q6UXY1; -.
DR PeptideAtlas; Q6UXY1; -.
DR PRIDE; Q6UXY1; -.
DR ProteomicsDB; 67675; -. [Q6UXY1-1]
DR ProteomicsDB; 67676; -. [Q6UXY1-2]
DR ABCD; Q6UXY1; 4 sequenced antibodies.
DR Antibodypedia; 301; 144 antibodies from 25 providers.
DR DNASU; 80115; -.
DR Ensembl; ENST00000381669.8; ENSP00000371085.3; ENSG00000128298.18. [Q6UXY1-1]
DR GeneID; 80115; -.
DR KEGG; hsa:80115; -.
DR MANE-Select; ENST00000381669.8; ENSP00000371085.3; NM_025045.6; NP_079321.3.
DR UCSC; uc003auw.4; human. [Q6UXY1-1]
DR CTD; 80115; -.
DR DisGeNET; 80115; -.
DR GeneCards; BAIAP2L2; -.
DR HGNC; HGNC:26203; BAIAP2L2.
DR HPA; ENSG00000128298; Group enriched (intestine, kidney).
DR MIM; 617536; gene.
DR neXtProt; NX_Q6UXY1; -.
DR OpenTargets; ENSG00000128298; -.
DR PharmGKB; PA142672563; -.
DR VEuPathDB; HostDB:ENSG00000128298; -.
DR eggNOG; ENOG502QW6V; Eukaryota.
DR GeneTree; ENSGT00940000153560; -.
DR HOGENOM; CLU_025877_1_1_1; -.
DR InParanoid; Q6UXY1; -.
DR OMA; MIQTKAP; -.
DR OrthoDB; 457637at2759; -.
DR PhylomeDB; Q6UXY1; -.
DR TreeFam; TF325648; -.
DR PathwayCommons; Q6UXY1; -.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 80115; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; BAIAP2L2; human.
DR GenomeRNAi; 80115; -.
DR Pharos; Q6UXY1; Tbio.
DR PRO; PR:Q6UXY1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6UXY1; protein.
DR Bgee; ENSG00000128298; Expressed in mucosa of transverse colon and 125 other tissues.
DR ExpressionAtlas; Q6UXY1; baseline and differential.
DR Genevisible; Q6UXY1; HS.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
DR GO; GO:0071439; C:clathrin complex; IDA:dictyBase.
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; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid 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:0061024; P:membrane organization; ISS: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 Alternative splicing; Cell junction; Cell membrane; Cytoplasmic vesicle;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..529
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2-like protein 2"
FT /id="PRO_0000256130"
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 221..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT VAR_SEQ 441..454
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021324"
FT CONFLICT 252
FT /note="C -> R (in Ref. 3; AAH15619)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="M -> MTPM (in Ref. 3; AAH15619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 58987 MW; A9D16724F6FCE118 CRC64;
MAPEMDQFYR STMAIYKSIM EQFNPALENL VYLGNNYLRA FHALSEAAEV YFSAIQKIGE
RALQSPTSQI LGEILVQMSD TQRHLNSDLE VVVQTFHGGL LQHMEKNTKL DMQFIKDSRQ
HYELEYRHRA ANLEKCMSEL WRMERKRDKN VREMKESVNR LHAQMQAFVS ESQRAAELEE
KRRYRFLAEK HLLLSNTFLQ FFGRARGMLQ NRVLLWKEQS EASRSPSRAH SPGLLGPALG
PPYPSGRLTP TCLDMPPRPL GEFSSPRSRH GSGSYGTEPD ARPASQLEPD RRSLPRTPSA
SSLYSGSAQS SRSNSFGERP GGGGGARRVR ALVSHSEGAN HTLLRFSAGD VVEVLVPEAQ
NGWLYGKLEG SSASGWFPEA YVKALEEGPV NPMTPVTPMT SMTSMSPMTP MNPGNELPSR
SYPLRGSHSL DDLLDRPGNS IAPSEYWDGQ SRSRTPSRVP SRAPSPAPPP LPSSRRSSMG
STAVATDVKK LMSSEQYPPQ ELFPRGTNPF ATVKLRPTIT NDRSAPLIR
