RIPR2_BOVIN
ID RIPR2_BOVIN Reviewed; 1016 AA.
AC Q3B7M3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Rho family-interacting cell polarization regulator 2 {ECO:0000250|UniProtKB:Q9Y4F9};
GN Name=RIPOR2 {ECO:0000250|UniProtKB:Q9Y4F9}; Synonyms=FAM65B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an inhibitor of the small GTPase RHOA and plays
CC several roles in the regulation of myoblast and hair cell
CC differentiation, lymphocyte T proliferation and neutrophil
CC polarization. Plays a role in fetal mononuclear myoblast
CC differentiation by promoting filopodia and myotube formation. Maintains
CC naive T lymphocytes in a quiescent state and prevents chemokine-induced
CC T lymphocyte responses, such as cell adhesion, polarization and
CC migration. Involved also in the regulation of neutrophil polarization,
CC chemotaxis and adhesion. Required for normal development of inner and
CC outer hair cell stereocilia within the cochlea of the inner ear. Plays
CC a role for maintaining the structural organization of the basal domain
CC of stereocilia. Involved in mechanosensory hair cell function. Required
CC for normal hearing. {ECO:0000250|UniProtKB:Q80U16,
CC ECO:0000250|UniProtKB:Q9Y4F9}.
CC -!- SUBUNIT: Homooligomer; homooligomerization is regulated by RHOC and
CC leads to the formation of concatemers through the association of N- and
CC C-termini (By similarity). Interacts (phosphorylated form) with 14-3-3
CC proteins; these interactions occur during myogenic cell differentiation
CC and also induces T cell proliferation arrest (By similarity). Interacts
CC (phosphorylated form) with HDAC6; this interaction occurs during early
CC myogenic differentiation, prevents HDAC6 to deacetylate tubulin and
CC also induces T cell proliferation arrest (By similarity). Interacts
CC with DYSF; this interaction occurs during early myogenic
CC differentiation (By similarity). Interacts with MYOF (By similarity).
CC Interacts (via active GTP- or inactive GDP-bound forms) with RHOA; this
CC interaction is direct, blocks the loading of GTP to RHOA and decreases
CC upon chemokine CCL19 stimulation in primary T lymphocytes. Interacts
CC with RHOC (By similarity). Interacts (via phosphorylated form) with
CC YWHAB; this interaction occurs in a chemokine-dependent manner and does
CC not compete for binding of RIPOR2 with RHOA nor blocks inhibition of
CC RIPOR2-mediated RHOA activity (By similarity). Interacts with YWHAE (By
CC similarity). Interacts with YWHAQ (By similarity).
CC {ECO:0000250|UniProtKB:Q80U16, ECO:0000250|UniProtKB:Q9Y4F9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4F9}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y4F9}. Cell
CC projection, filopodium {ECO:0000250|UniProtKB:Q9Y4F9}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q7TP54}. Cell projection, stereocilium
CC {ECO:0000250|UniProtKB:Q80U16}. Cell projection, stereocilium membrane
CC {ECO:0000250|UniProtKB:Q7TP54}. Note=Localized in the cytoplasm in
CC cells undergoing mitosis. Colocalized with F-actin. Accumulates at the
CC leading edge of polarized neutrophils in a chemokine-dependent manner.
CC Localized with RHOC within the basal domain of hair cell stereocilia,
CC near the taper region. Detected in punctate pattern forming a
CC circumferential ring at the stereocilia base. Localized to the apical
CC stereocilia of inner and outer hair cells.
CC {ECO:0000250|UniProtKB:Q7TP54, ECO:0000250|UniProtKB:Q80U16,
CC ECO:0000250|UniProtKB:Q9Y4F9}.
CC -!- PTM: Phosphorylated. Chemokine-induced phosphorylation in neutrophils
CC occurs in a PKC- and AKT-dependent manner, resulting in RIPOR2
CC interaction with YWHAB and stabilization. Phosphorylated by PKCA, AKT1
CC and MAPKAPK1A; in vitro. {ECO:0000250|UniProtKB:Q9Y4F9}.
CC -!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
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DR EMBL; BC107544; AAI07545.1; -; mRNA.
DR RefSeq; NP_001030502.1; NM_001035425.1.
DR AlphaFoldDB; Q3B7M3; -.
DR STRING; 9913.ENSBTAP00000024178; -.
DR PaxDb; Q3B7M3; -.
DR PRIDE; Q3B7M3; -.
DR GeneID; 539635; -.
DR KEGG; bta:539635; -.
DR CTD; 9750; -.
DR eggNOG; ENOG502QQ7T; Eukaryota.
DR InParanoid; Q3B7M3; -.
DR OrthoDB; 1121546at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:1903904; P:negative regulation of establishment of T cell polarity; ISS:UniProtKB.
DR GO; GO:1905872; P:negative regulation of protein localization to cell leading edge; ISS:UniProtKB.
DR GO; GO:2001107; P:negative regulation of Rho guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:2000405; P:negative regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR031780; FAM65_N.
DR InterPro; IPR033035; FAM65B.
DR InterPro; IPR026136; RIPOR3.
DR PANTHER; PTHR15829; PTHR15829; 2.
DR PANTHER; PTHR15829:SF2; PTHR15829:SF2; 2.
DR Pfam; PF15903; PL48; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Cell projection; Chemotaxis; Coiled coil;
KW Cytoplasm; Cytoskeleton; Differentiation; Hearing; Membrane; Myogenesis;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..1016
FT /note="Rho family-interacting cell polarization regulator
FT 2"
FT /id="PRO_0000289113"
FT REGION 44..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..113
FT /note="Involved in cell filopodia formation"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F9"
FT REGION 414..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..112
FT /evidence="ECO:0000255"
FT COMPBIAS 414..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F9"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F9"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F9"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U16"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F9"
SQ SEQUENCE 1016 AA; 111934 MW; 515DCF291B51034C CRC64;
MLVGSQSFSP GGPNGIIRSQ SFAGFSGLQE RRSRCNSFIE NSSAVKKPQA KLKKMHNLGH
KNSSPPKEPQ PKRVEEVYRA LKNGLDEYLE VHQTELDKLT TQLKDMRRNS RLGVLYDLDK
QIKTIERYMR RLEFHISKVD ELYEAYCIQR RLQDGASKMK QAFATSPASK AARESLAEIN
RSYKEYTENM CAIEAELEKQ LGEFSIKMKG LAGFARLCPG DQYEIFMKYG RQRWKLKGRI
EVNGKQSWDG EEMVFLPLIV GFISIKVTEL KGLATHLLVG SVTCETKELF AARPQVVAVD
INDLGTIKLN LEITWYPFDV EDMTPSSGAG NKVAALQRRM SMYSQGTPET PTFKDHSFFS
NLPDDIFENG KAAEEKMPLS LSFSDLPNGD CTLAPGPADS LPGACAANPE ITITSTELPP
GSQSSQNEGL KDSSSASCSS SSREGSEPRP HPEGETQGLG KPEGCPVATG ARPERLFLQK
GVAEALLQEA LLQEPSELKP VELDTFEGNI TKQLVKRLTS AEVPAATERL LSEGSISAES
EGCRSFLDGS LEDAFNGLFL ALEPHKEQYK EFQDLNQEVM HLDDILKCKP AVSRSRSSSL
SLTVESALES FDFLNTSDFD EEEDGDEVCN VGGGADSVFS DTETEKNSYR SVHPEARGHL
SEALTEDTGV GTSVAGSPLP LTTGNESLDL TIIRHLQYCT QLVQQIVLSS KTPFVASNLL
EKLSRQIQVM EKLSAVSDEN IGNISSVIEA IPEFHKKLSL LSFWTKCCTP IGVYHSSADR
VIKQLEASFA RTVNRDYPGL ADPVFHTLVS QILDRAEPLL PASLSSEVIT VFQYYSYFTS
HGVSDLESYL NQLAKQVSVV QTLQSLRDEK LLQAVSDLAP GSFPAPQEEV LRTLALLLTG
EDSGASEAVT LYLTAASRSE HFREKALLYY CEALTKTDFR LQKAACLALK SLKATESIKM
LVTLCQSDTE EIRNVASETL LSLGEDGRLA YEQLDKFPRD CVKVGGRLAS EVATAF
