REPS2_MOUSE
ID REPS2_MOUSE Reviewed; 647 AA.
AC Q80XA6; A2AFI8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=RalBP1-associated Eps domain-containing protein 2;
DE AltName: Full=Partner of RalBP1;
DE AltName: Full=RalBP1-interacting protein 2;
GN Name=Reps2; Synonyms=Pob1;
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].
RC STRAIN=C57BL/6J;
RA Huang K.M., Geunes-Boyer S., Stambolian D., Dutra A., Favor J.;
RT "Organization and annotation of the Xcat critical region and elimination of
RT three candidate genes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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 MRNA].
RC TISSUE=Brain;
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 INTERACTION WITH ASAP1.
RX PubMed=12149250; DOI=10.1074/jbc.m203453200;
RA Oshiro T., Koyama S., Sugiyama S., Kondo A., Onodera Y., Asahara T.,
RA Sabe H., Kikuchi A.;
RT "Interaction of POB1, a downstream molecule of small G protein Ral, with
RT PAG2, a paxillin-binding protein, is involved in cell migration.";
RL J. Biol. Chem. 277:38618-38626(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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: Involved in ligand-dependent receptor mediated endocytosis of
CC the EGF and insulin receptors as part of the Ral signaling pathway (By
CC similarity). By controlling growth factor receptors endocytosis may
CC regulate cell survival (By similarity). Through ASAP1 may regulate cell
CC adhesion and migration (By similarity). {ECO:0000250|UniProtKB:Q8NFH8}.
CC -!- SUBUNIT: Interacts with EPN1 (By similarity). Interacts with EPS15 AND
CC EPS15L1 (By similarity). Interacts with RALBP1; can form a ternary
CC complex with activated Ral (RALA or RALB) (By similarity). Interacts
CC with ASAP1; the interaction is direct and this complex can bind
CC paxillin (PubMed:12149250). Also forms a ternary complex with RALBP1
CC and ASAP1 (By similarity). Interacts with GRB2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8NFH8, ECO:0000269|PubMed:12149250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NFH8}.
CC -!- PTM: Tyrosine-phosphorylated upon stimulation of cells with EGF.
CC Phosphorylation on Tyr-residues induces its association with the EGF
CC receptor probably indirectly through an adapter like GRB2.
CC {ECO:0000250|UniProtKB:Q8NFH8}.
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DR EMBL; AY263368; AAO92604.1; -; mRNA.
DR EMBL; AL672039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145500; AAI45501.1; -; mRNA.
DR CCDS; CCDS72462.1; -.
DR RefSeq; NP_001277562.1; NM_001290633.1.
DR RefSeq; NP_839987.2; NM_178256.4.
DR RefSeq; XP_006528825.1; XM_006528762.3.
DR AlphaFoldDB; Q80XA6; -.
DR SMR; Q80XA6; -.
DR BioGRID; 228794; 9.
DR STRING; 10090.ENSMUSP00000098661; -.
DR iPTMnet; Q80XA6; -.
DR EPD; Q80XA6; -.
DR jPOST; Q80XA6; -.
DR MaxQB; Q80XA6; -.
DR PaxDb; Q80XA6; -.
DR PeptideAtlas; Q80XA6; -.
DR PRIDE; Q80XA6; -.
DR ProteomicsDB; 253114; -.
DR ProteomicsDB; 332930; -.
DR Antibodypedia; 434; 118 antibodies from 27 providers.
DR Ensembl; ENSMUST00000112334; ENSMUSP00000107953; ENSMUSG00000040855.
DR GeneID; 194590; -.
DR KEGG; mmu:194590; -.
DR UCSC; uc012hri.2; mouse.
DR CTD; 9185; -.
DR MGI; MGI:2663511; Reps2.
DR VEuPathDB; HostDB:ENSMUSG00000040855; -.
DR eggNOG; KOG1955; Eukaryota.
DR GeneTree; ENSGT00940000158080; -.
DR InParanoid; Q80XA6; -.
DR OrthoDB; 1319710at2759; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 194590; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Reps2; mouse.
DR PRO; PR:Q80XA6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q80XA6; protein.
DR Bgee; ENSMUSG00000040855; Expressed in medial dorsal nucleus of thalamus and 178 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR Pfam; PF12763; EF-hand_4; 1.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 1.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..647
FT /note="RalBP1-associated Eps domain-containing protein 2"
FT /id="PRO_0000073832"
FT DOMAIN 21..122
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 268..359
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 301..336
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 156..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..647
FT /note="Interaction with RALBP1"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH8"
FT REGION 548..647
FT /note="Interaction with ASAP1"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH8"
FT COILED 599..640
FT /evidence="ECO:0000255"
FT COMPBIAS 186..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..513
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH8"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH8"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH8"
SQ SEQUENCE 647 AA; 70484 MW; 85303F400FEBD533 CRC64;
MEVAAGGGCG AGPPLLLSDS EQQCYSELFA RCAGAASGGP GPGPPEATRV APGTATAAAG
PVADLFRASQ LPPETLHQIT ELCGAKRVGY FGPTQFYVAL KLIAAAQAGL PVRTESIKCE
LPLPRFVMSK NDGEIRFGNP AELHGPKVQI PYLTTEKNSF KRMDNEDKQE TQSPTMSPLA
SPPSSPPHYQ RVSLSHGYSK LRSGTEQMHP APYERQPIGQ PEGPSSEGPG AKPFRRQASL
IRSFSVEREP QENNSNYPDE PWRITEEQRE YYVNQFRSLQ PDPSSFISGS VAKNFFTKSK
LSIPELSYIW ELSDADCDGA LTLSEFCAAF HLIVARKNGY PLPEGLPPTL QPEYLQAAFP
KSKWECAIFD SYSESMPANQ QSCDLNRMEK TSVKDVADFP VPTQDVTTAD DKQALKSTVN
ESLPKDVSED TATSKDYNSL KARPRSRSYS STSIEEAMKR GEDPPTPPPR PQKTHSRASS
LDLNKVFLPS APAANSGLLP PPPALPPRPC PTQSEPVSEA DLHSQLNRAP SQAAESSPTK
MDAPHAQPPS KPIRRKFRPE NQTTESQEPA AAVGGAVSAA MVKPHPTVQK QSSKQKKAIQ
TAIRKNKEAN AVLARLNSEL QQQLKEVHQE RIALENQLEQ LRPVTVL
