ID   RIPR2_CHICK             Reviewed;         602 AA.
AC   Q5F3L9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Rho family-interacting cell polarization regulator 2 {ECO:0000250|UniProtKB:Q9Y4F9};
DE   AltName: Full=Myogenesis-related and NCAM-associated protein;
GN   Name=RIPOR2 {ECO:0000250|UniProtKB:Q9Y4F9}; Synonyms=FAM65B, MYONAP;
GN   ORFNames=RCJMB04_13m20;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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:A9ZLX4,
CC       ECO:0000250|UniProtKB:Q80U16, 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. Interacts with NCAM. {ECO:0000250|UniProtKB:A9ZLX4,
CC       ECO:0000250|UniProtKB:Q80U16}.
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}.
CC   -!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
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DR   EMBL; AJ851631; CAH65265.1; -; mRNA.
DR   RefSeq; NP_001012883.1; NM_001012865.1.
DR   AlphaFoldDB; Q5F3L9; -.
DR   SMR; Q5F3L9; -.
DR   STRING; 9031.ENSGALP00000022126; -.
DR   PaxDb; Q5F3L9; -.
DR   GeneID; 421003; -.
DR   KEGG; gga:421003; -.
DR   CTD; 421003; -.
DR   VEuPathDB; HostDB:geneid_421003; -.
DR   eggNOG; ENOG502QQ7T; Eukaryota.
DR   InParanoid; Q5F3L9; -.
DR   OrthoDB; 1121546at2759; -.
DR   PhylomeDB; Q5F3L9; -.
DR   PRO; PR:Q5F3L9; -.
DR   Proteomes; UP000000539; 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   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.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Cell projection; Chemotaxis; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Differentiation; Hearing; Membrane; Myogenesis;
KW   Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..602
FT                   /note="Rho family-interacting cell polarization regulator
FT                   2"
FT                   /id="PRO_0000345985"
FT   REGION          46..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..421
FT                   /note="Necessary for interaction with NCAM and myoblast
FT                   protrusion formation"
FT                   /evidence="ECO:0000250|UniProtKB:A9ZLX4"
FT   REGION          384..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          83..112
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        400..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  66897 MW;  6B4085873BB34B11 CRC64;
     MSIGSHSFSP GGPNGIIRSQ SFAGFSGLQE RRSRCNSFIE NSSALKKPQA KVKKMHNLGH
     KNSTTPKEPQ PKRMEEVYRA LKNGLDEYLE VHQTELDKLT AQLKDMRRNS RLGVLYDLDK
     QIKAVERYMR RLEFHISKVD ELYEAYCIQR RLCDGASKMK QAFAMSPASK AARESLTEIN
     RSYKEYTENM CTIEAELENL LGEFCIKMKG LAGFARLCPG DQYEIFMRYG RQRWKLKGKI
     EVNGKQSWDG EEMVFLPLIV GLISIKVTEV KGLATHILVG SVTCETKDLF AARPQVVAVD
     INDLGTIKLN LEITWYPFDV EDLTPSTANV SKASALQRRM SMYSQGTPET PTFKDHSFFS
     NLPDDVFENG TAATEKRPLS FTFGDLPYED RVPPANPAEP SSAHVSSSPD ITTAATQHRA
     LKSSESSSPD CSSSDSCGDA VPEPKDLPSP GEAVVTGNKV TPRARSEVCQ KPSNAGSDRV
     FIEANVPVSL LQDTDEGSEL KPVELDTYEG NITKQLVKRL TSAEVPGTPE RLPCEGSISG
     ESEGYKSYLD GSIEEALQGL LLALEPHKEQ YKEFQDLDQE VMHLDDILKV STFSESTTLK
     DI