RIPR2_COTJA
ID RIPR2_COTJA Reviewed; 1072 AA.
AC A9ZLX4; A9ZLZ2; A9ZLZ3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Rho family-interacting cell polarization regulator 2 {ECO:0000250|UniProtKB:Q9Y4F9};
DE AltName: Full=Myogenesis-related and NCAM-associated protein {ECO:0000303|PubMed:17825087};
GN Name=RIPOR2 {ECO:0000250|UniProtKB:Q9Y4F9};
GN Synonyms=FAM65B, MYONAP {ECO:0000303|PubMed:17825087};
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NCAM, AND DOMAIN.
RX PubMed=17825087; DOI=10.1111/j.1432-0436.2007.00215.x;
RA Hirayama E., Kim J.;
RT "Identification and characterization of a novel neural cell adhesion
RT molecule (NCAM)-associated protein from quail myoblasts: relationship to
RT myotube formation and induction of neurite-like protrusions.";
RL Differentiation 76:253-266(2008).
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
CC (PubMed:17825087). Maintains naive T lymphocytes in a quiescent state
CC and prevents chemokine-induced T lymphocyte responses, such as cell
CC adhesion, polarization and migration. Involved also in the regulation
CC of neutrophil polarization, chemotaxis and adhesion. Required for
CC normal development of inner and outer hair cell stereocilia within the
CC cochlea of the inner ear. Plays a role for maintaining the structural
CC organization of the basal domain of stereocilia. Involved in
CC mechanosensory hair cell function. Required for normal hearing (By
CC similarity). {ECO:0000250|UniProtKB:Q80U16,
CC ECO:0000250|UniProtKB:Q9Y4F9, ECO:0000269|PubMed:17825087}.
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. Interacts with NCAM; this interaction is necessary for
CC myoblast protrusion formation (PubMed:17825087).
CC {ECO:0000250|UniProtKB:Q80U16, ECO:0000269|PubMed:17825087}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17825087}.
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A9ZLX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A9ZLX4-2; Sequence=VSP_034972, VSP_034973, VSP_034974,
CC VSP_034975;
CC Name=3;
CC IsoId=A9ZLX4-3; Sequence=VSP_034969, VSP_034970, VSP_034971;
CC -!- TISSUE SPECIFICITY: Expressed in myoblast and myotubes (at protein
CC level). Expressed in brain, eyes and skeletal muscle.
CC {ECO:0000269|PubMed:17825087}.
CC -!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
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DR EMBL; AB128922; BAF96640.1; -; mRNA.
DR EMBL; AB169974; BAF96641.1; -; mRNA.
DR EMBL; AB182319; BAF96642.1; -; mRNA.
DR AlphaFoldDB; A9ZLX4; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IMP:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IMP: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; 1.
DR PANTHER; PTHR15829:SF2; PTHR15829:SF2; 1.
DR Pfam; PF15903; PL48; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Chemotaxis; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Hearing;
KW Membrane; Myogenesis; Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..1072
FT /note="Rho family-interacting cell polarization regulator
FT 2"
FT /id="PRO_0000345986"
FT REGION 173..470
FT /note="Necessary for interaction with NCAM and myoblast
FT protrusion formation"
FT /evidence="ECO:0000269|PubMed:17825087"
FT REGION 439..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..112
FT /evidence="ECO:0000255"
FT COMPBIAS 448..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1
FT /note="M -> MERRLCPRSPGLRRQRAKHVPGCAVSRGDTAIAAGISSRLPEIM
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17825087"
FT /id="VSP_034969"
FT VAR_SEQ 243..251
FT /note="NGKQSWDGE -> LKKPCKGFS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17825087"
FT /id="VSP_034970"
FT VAR_SEQ 252..1072
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17825087"
FT /id="VSP_034971"
FT VAR_SEQ 360..408
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17825087"
FT /id="VSP_034972"
FT VAR_SEQ 470..506
FT /note="RAQTAAAVTPAEGKACPGVRCEPRGHGDSCQEYPPGF -> LKSSESSSPDC
FT SSSDSCRDSIPEPKDLPSPREAAATRNKATPRAHAEVC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17825087"
FT /id="VSP_034973"
FT VAR_SEQ 627..639
FT /note="CKPAVSRSRSSSL -> VSTFSESTTLEEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17825087"
FT /id="VSP_034974"
FT VAR_SEQ 640..1072
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17825087"
FT /id="VSP_034975"
FT CONFLICT 168
FT /note="T -> A (in Ref. 1; BAF96642)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="T -> I (in Ref. 1; BAF96641)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="R -> C (in Ref. 1; BAF96641)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="E -> G (in Ref. 1; BAF96641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1072 AA; 119322 MW; BF38BC132D200BA5 CRC64;
MSIGSHSFSP GGPNGIIRSQ SFAGFSGLQE RRSRCNSFIE NTSALKKPQA KVKKMHNLGH
KNSTTPKEPQ PKRVEEVYRA LKNGLDEYLE VHQTELDKLT AQLKDMRRNS RLGVLYDLDK
QIKAVERYMR RLEFHISKVD ELYEAYCIQR RLCDGASKMK QAFAMSPTSK AARESLTEIN
RSYKEYTENM CTIEAELENL LGEFCIKMKG LAGFARLCPG DQYEIFMRYG RQRWKLKGKI
EVNGKQSWDG EEMVFLPLIV GLISIKVTEV KGLATHILVG SVTCETKDLF AARPQVVAVD
INDLGTIKLN LEITWYPFDV EDLTPSTGNV SKASALQRRM SMYSQGTPET PTFKDHSFFR
WLHPLQDRPR LAILDALQDT FFDKLRRSRS FSDLPSLRLS PKAGLELYSN LPDDVFENGT
ATTEKRPLSF TFGDLPYEDR VPPANSAEPS SAHVTSSPDI ATTATQHRAR AQTAAAVTPA
EGKACPGVRC EPRGHGDSCQ EYPPGFQKPS DTGSDRVFIE ANVPVSLLQD TDEGSELKPV
ELDTYEGNIT KQLVKRLTSA EVPGTPERLP CEGSISGESE GYKSYLDGSI EEALQGLLLA
LEPHKEQYKE FQDLDQEVMH LDDILKCKPA VSRSRSSSLS LTVESALESF DFLNTSDFDD
EDGGGEEVCN GGGGADSVFS DTEVEKNSYR TEHPEARGHL QRSLTEDTGV GTSVAGSPLP
LTTGSDSLDI TIVKHLQYCT QLIQQIVFSR KTPFVTRDLL DKLSRQTLVM ENIAEISTEN
LGSITSLTDA IPEFHKKLSL LAFWMKCTGP SGVYHTSADK MMKQLDINFA ATVNEECPGL
AETVFRILVS QILDRTEPVL YSTMSSEIIT VFQYYNYFAS HSVNDLGSYL LQLAKEASVV
QMLQSVKDGK LQQNVSKINS NNLPPQQEVL RALALLLNEN KNEVSETVAS LLTATAENKH
FREKALIYYC EALTQPNLQL QKAACLALRY LKATESIKML VMLCQSDNEE IRKVASETLL
SLGEDGRLAY EQLDNSPGNL SELEVAGELN LPQLSRRTCL SVTATEEGWS CH
