ID AB1IP_MOUSE Reviewed; 670 AA.
AC Q8R5A3; O35329; Q8BRU0; Q99KV8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Amyloid beta A4 precursor protein-binding family B member 1-interacting protein;
DE AltName: Full=APBB1-interacting protein 1;
DE AltName: Full=Proline-rich EVH1 ligand 1;
DE Short=PREL-1;
DE AltName: Full=Proline-rich protein 48;
GN Name=Apbb1ip; Synonyms=Prel1;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH ENAH; VASP AND RAP1A.
RC TISSUE=Cervix carcinoma;
RX PubMed=15642358; DOI=10.1016/j.febslet.2004.10.110;
RA Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.;
RT "PREL1 provides a link from Ras signalling to the actin cytoskeleton via
RT Ena/VASP proteins.";
RL FEBS Lett. 579:455-463(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-282.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-670, TISSUE SPECIFICITY, AND INTERACTION
RP WITH APBB1.
RX PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
RA Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T.,
RA Sudol M.;
RT "The WW domain of neural protein FE65 interacts with proline-rich motifs in
RT Mena, the mammalian homolog of Drosophila enabled.";
RL J. Biol. Chem. 272:32869-32877(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; THR-534 AND SER-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, and Spleen;
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).
CC -!- FUNCTION: Appears to function in the signal transduction from Ras
CC activation to actin cytoskeletal remodeling. Suppresses insulin-induced
CC promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts, through the N-terminal Pro-rich region, with the WW
CC domain of APBB1. Interacts with RAP1A, PFN1, VASP and ENAH.
CC {ECO:0000269|PubMed:15642358, ECO:0000269|PubMed:9407065}.
CC -!- INTERACTION:
CC Q8R5A3; P26039: Tln1; NbExp=8; IntAct=EBI-7450496, EBI-1039593;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15642358};
CC Peripheral membrane protein {ECO:0000269|PubMed:15642358}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:15642358}. Cell junction,
CC focal adhesion {ECO:0000269|PubMed:15642358}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15642358}. Note=Colocalizes with ENA/VASP proteins
CC at lamellipodia tips and focal adhesions, and F-actin at the leading
CC edge. At the membrane surface, associates, via the PH domain,
CC preferentially with the inositol phosphates, PtdIns(5)P and PtdIns(3)P.
CC This binding appears to be necessary for the efficient interaction of
CC the RA domain to Ras-GTPases.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in the
CC hematopoietic system. {ECO:0000269|PubMed:15642358,
CC ECO:0000269|PubMed:9407065}.
CC -!- SIMILARITY: Belongs to the MRL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB94880.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC003991; AAH03991.1; -; mRNA.
DR EMBL; BC023110; AAH23110.1; -; mRNA.
DR EMBL; AK041552; BAC30983.1; -; mRNA.
DR EMBL; AF020313; AAB94880.1; ALT_FRAME; mRNA.
DR CCDS; CCDS38056.1; -.
DR RefSeq; NP_062329.2; NM_019456.2.
DR RefSeq; XP_006498249.1; XM_006498186.2.
DR RefSeq; XP_011237441.1; XM_011239139.2.
DR PDB; 3TCA; X-ray; 2.35 A; A/B=150-437.
DR PDB; 4KVG; X-ray; 1.65 A; B/D=179-437.
DR PDB; 4W8P; X-ray; 1.50 A; B=5-25.
DR PDB; 6O6H; X-ray; 2.50 A; A=150-437.
DR PDB; 6OLU; X-ray; 1.90 A; A=179-437.
DR PDB; 7V1A; X-ray; 1.84 A; B=7-25.
DR PDBsum; 3TCA; -.
DR PDBsum; 4KVG; -.
DR PDBsum; 4W8P; -.
DR PDBsum; 6O6H; -.
DR PDBsum; 6OLU; -.
DR PDBsum; 7V1A; -.
DR AlphaFoldDB; Q8R5A3; -.
DR BMRB; Q8R5A3; -.
DR SMR; Q8R5A3; -.
DR BioGRID; 207671; 6.
DR DIP; DIP-29358N; -.
DR IntAct; Q8R5A3; 2.
DR MINT; Q8R5A3; -.
DR STRING; 10090.ENSMUSP00000014290; -.
DR iPTMnet; Q8R5A3; -.
DR PhosphoSitePlus; Q8R5A3; -.
DR SwissPalm; Q8R5A3; -.
DR EPD; Q8R5A3; -.
DR jPOST; Q8R5A3; -.
DR MaxQB; Q8R5A3; -.
DR PaxDb; 10090-ENSMUSP00000014290; -.
DR ProteomicsDB; 296433; -.
DR Pumba; Q8R5A3; -.
DR Antibodypedia; 38122; 284 antibodies from 30 providers.
DR DNASU; 54519; -.
DR Ensembl; ENSMUST00000014290.15; ENSMUSP00000014290.9; ENSMUSG00000026786.15.
DR GeneID; 54519; -.
DR KEGG; mmu:54519; -.
DR UCSC; uc008inn.2; mouse.
DR AGR; MGI:1861354; -.
DR CTD; 54518; -.
DR MGI; MGI:1861354; Apbb1ip.
DR VEuPathDB; HostDB:ENSMUSG00000026786; -.
DR eggNOG; KOG3751; Eukaryota.
DR GeneTree; ENSGT00940000156105; -.
DR HOGENOM; CLU_023207_2_0_1; -.
DR InParanoid; Q8R5A3; -.
DR OMA; CCDDQAT; -.
DR OrthoDB; 3144731at2759; -.
DR PhylomeDB; Q8R5A3; -.
DR TreeFam; TF317511; -.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR BioGRID-ORCS; 54519; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Apbb1ip; mouse.
DR PRO; PR:Q8R5A3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R5A3; Protein.
DR Bgee; ENSMUSG00000026786; Expressed in granulocyte and 113 other cell types or tissues.
DR ExpressionAtlas; Q8R5A3; baseline and differential.
DR Genevisible; Q8R5A3; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042101; C:T cell receptor complex; IDA:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IDA:MGI.
DR CDD; cd01259; PH_APBB1IP; 1.
DR CDD; cd16137; RA_MRL_RIAM; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR039664; GRB/APBB1IP.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR039665; PH_APBB1IP.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11243:SF14; AMYLOID BETA A4 PRECURSOR PROTEIN-BINDING FAMILY B MEMBER 1-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR11243; GROWTH FACTOR RECEPTOR-BOUND PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..670
FT /note="Amyloid beta A4 precursor protein-binding family B
FT member 1-interacting protein"
FT /id="PRO_0000181348"
FT DOMAIN 179..266
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 313..422
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 449..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 66..69
FT /note="ALMA -> EFKP (in Ref. 4; AAB94880)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="A -> D (in Ref. 2; AAH03991)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="Missing (in Ref. 1, 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="Missing (in Ref. 1, 2; AAH23110 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="S -> P (in Ref. 2; AAH03991)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="T -> S (in Ref. 2; AAH03991)"
FT /evidence="ECO:0000305"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:4W8P"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:4KVG"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:4KVG"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:4KVG"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6OLU"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 407..422
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:4KVG"
SQ SEQUENCE 670 AA; 74319 MW; 39EB28E468C479C8 CRC64;
MGESNEDIDQ MFSTLLGEMD LLTQSLGVDT LPPPDPNPPR EEFNYTVGFK DLNESLNALE
DQDLDALMAD LVADISEAEQ RTIQAQKESS QNQDRFALLR ASDGQGTASG GYGASAAAID
VSHHEEALPP PPVEPMLDLL PPPPPPPPPE LLSKEEEEAK AKADKIKLAL EKLKEAKVKK
LVVKVHMDDS STKSLMVDER QLARDVLDNL FEKTHCDCNV DWCLYEIYPE LQIERVFEDH
ENVVEVLSDW TRDTENKVLF LEKEERYAVF KNPQNFYLDN KGKKENKETN EKMNAKNKEY
LLEESFCGTS IIVPELEGAL YLKEDGKKSW KRRYFLLRAS GIYYVPKGKT KTSRDLACFI
QFENVNIYYG IQCKMKYKAP TDHCFVLKHP QIQKESQYIK YLCCDDARTL SQWVMGIRIA
KYGKTLYDNY QRAVARAGLA SRWTNLGTVG TPMPAQPSTV SSGLKTGTSQ PNGQMPQAIP
SAGPPLQEAQ TQIETTKDEK QGLGNHSPGA TRENHRPKSS LPPPPPPVRR SSDTCGSPAL
PSKVKGPGTC TFPHPPENFL PPPPPPPPEE DNSGLLPPPP PPPYLEEPPD FVPPPPPPAA
VEDSALPPPP PPPPCLSQEI TKSSPLPPKK PLVPPKRQEN QGLPGAPGNS EQDFMSDLMK
ALQKKRGNIP
//
