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Rho family-interacting cell polarization regulator 2

 RIPR2_HUMAN             Reviewed;        1068 AA.
Q9Y4F9; A6NHP2; Q13529; Q5VV37; Q5VV38; Q9BQ28;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 4.
22-NOV-2017, entry version 126.
RecName: Full=Rho family-interacting cell polarization regulator 2;
Name=RIPOR2;
Synonyms=C6orf32, DIFF48, FAM65B, KIAA0386,
PL48 {ECO:0000303|PubMed:9055809};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Placenta;
PubMed=9055809; DOI=10.1016/S0378-1119(96)00587-2;
Dakour J., Li H., Morrish D.W.;
"PL48: a novel gene associated with cytotrophoblast and lineage-
specific HL-60 cell differentiation.";
Gene 185:153-157(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
MET-320 AND GLN-868.
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[3]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
POSSIBLE GLYCOSYLATION [LARGE SCALE ANALYSIS].
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
FUNCTION (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
DOMAIN.
PubMed=17150207; DOI=10.1016/j.ydbio.2006.11.002;
Yoon S., Molloy M.J., Wu M.P., Cowan D.B., Gussoni E.;
"C6ORF32 is upregulated during muscle cell differentiation and induces
the formation of cellular filopodia.";
Dev. Biol. 301:70-81(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[10]
FUNCTION, INTERACTION WITH RHOA (ISOFORMS 1 AND 2), SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INDUCTION (ISOFORMS 1 AND 2).
PubMed=23241886; DOI=10.4049/jimmunol.1201174;
Rougerie P., Largeteau Q., Megrelis L., Carrette F., Lejeune T.,
Toffali L., Rossi B., Zeghouf M., Cherfils J., Constantin G.,
Laudanna C., Bismuth G., Mangeney M., Delon J.;
"Fam65b is a new transcriptional target of FOXO1 that regulates RhoA
signaling for T lymphocyte migration.";
J. Immunol. 190:748-755(2013).
[11]
FUNCTION, TISSUE SPECIFICITY, ACETYLATION, SUBCELLULAR LOCATION,
INTERACTION WITH 14-3-3 PROTEINS; HDAC6; DYSF AND MYOF, AND INDUCTION.
PubMed=24687993; DOI=10.1096/fj.13-246470;
Balasubramanian A., Kawahara G., Gupta V.A., Rozkalne A., Beauvais A.,
Kunkel L.M., Gussoni E.;
"Fam65b is important for formation of the HDAC6-dysferlin protein
complex during myogenic cell differentiation.";
FASEB J. 28:2955-2969(2014).
[12]
FUNCTION, AND INVOLVEMENT IN DFNB104.
PubMed=24958875; DOI=10.1073/pnas.1401950111;
Diaz-Horta O., Subasioglu-Uzak A., Grati M., DeSmidt A., Foster J.,
Cao L., Bademci G., Tokgoz-Yilmaz S., Duman D., Cengiz F.B., Abad C.,
Mittal R., Blanton S., Liu X.Z., Farooq A., Walz K., Lu Z., Tekin M.;
"FAM65B is a membrane-associated protein of hair cell stereocilia
required for hearing.";
Proc. Natl. Acad. Sci. U.S.A. 111:9864-9868(2014).
[13]
FUNCTION (ISOFORM 2), INTERACTION WITH 14-3-3 PROTEINS; RHOA; YWHAB;
YWHAE AND YWHAQ (ISOFORM 2), PHOSPHORYLATION AT SER-21; SER-37;
SER-341; SER-523 AND SER-585 (ISOFORM 2), SUBCELLULAR LOCATION
(ISOFORM 2), MUTAGENESIS OF SER-21; SER-37; 151-ARG-LEU-152;
155-GLY-ALA-156; SER-341; SER-523 AND SER-585, AND IDENTIFICATION BY
MASS SPECTROMETRY (ISOFORM 2).
PubMed=25588844; DOI=10.1242/jcs.161497;
Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
"Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
leading edges polarizes neutrophils.";
J. Cell Sci. 128:992-1000(2015).
[14]
FUNCTION (ISOFORM 2), INTERACTION WITH 14-3-3 PROTEINS AND HDAC6
(ISOFORM 2), PHOSPHORYLATION (ISOFORM 2), MUTAGENESIS OF SER-21;
SER-37; 151-ARG-LEU-152; SER-341; SER-523 AND SER-585, INDUCTION
(ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
PubMed=27556504; DOI=10.18632/oncotarget.11438;
Froehlich J., Versapuech M., Megrelis L., Largeteau Q., Meunier S.,
Tanchot C., Bismuth G., Delon J., Mangeney M.;
"FAM65B controls the proliferation of transformed and primary T
cells.";
Oncotarget 7:63215-63225(2016).
-!- FUNCTION: Acts as an inhibitor of the small GTPase RHOA and plays
several roles in the regulation of myoblast and hair cell
differentiation, lymphocyte T proliferation and neutrophil
polarization (PubMed:17150207, PubMed:24687993, PubMed:23241886,
PubMed:24958875, PubMed:25588844, PubMed:27556504). Inhibits
chemokine-induced T lymphocyte responses, such as cell adhesion,
polarization and migration (PubMed:23241886). Involved also in the
regulation of neutrophil polarization, chemotaxis and adhesion (By
similarity). Required for normal development of inner and outer
hair cell stereocilia within the cochlea of the inner ear (By
similarity). Plays a role for maintaining the structural
organization of the basal domain of stereocilia (By similarity).
Involved in mechanosensory hair cell function (By similarity).
Required for normal hearing (PubMed:24958875).
{ECO:0000250|UniProtKB:Q80U16, ECO:0000269|PubMed:17150207,
ECO:0000269|PubMed:23241886, ECO:0000269|PubMed:24687993,
ECO:0000269|PubMed:24958875, ECO:0000269|PubMed:27556504}.
-!- FUNCTION: Isoform 2: Acts as an inhibitor of the small GTPase RHOA
(PubMed:25588844). Plays a role in fetal mononuclear myoblast
differentiation by promoting filopodia and myotube formation
(PubMed:17150207). Maintains naive T lymphocytes in a quiescent
state (PubMed:27556504). {ECO:0000269|PubMed:17150207,
ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27556504}.
-!- SUBUNIT: Homooligomer; homooligomerization is regulated by RHOC
and leads to the formation of concatemers through the association
of N- and C-termini (By similarity). Interacts with 14-3-3
proteins; these interactions occur during myogenic cell
differentiation (PubMed:24687993). Interacts with HDAC6; this
interaction occurs during early myogenic differentiation and
prevents HDAC6 to deacetylate tubulin (PubMed:24687993). Interacts
with DYSF; this interaction occurs during early myogenic
differentiation (PubMed:24687993). Interacts with MYOF
(PubMed:24687993). Interacts with RHOC (By similarity). Isoform 1
and isoform 2 interact (via active GTP- or inactive GDP-bound
forms) with RHOA; these interactions are direct, block the loading
of GTP to RHOA and decrease upon chemokine CCL19 stimulation in
primary T lymphocytes (PubMed:23241886, PubMed:25588844). Isoform
2 interacts (phosphorylated form) with HDAC6; this interaction
induces T cell proliferation arrest (PubMed:27556504). Isoform 2
interacts (phosphorylated form) with 14-3-3 proteins; these
interactions induces T cell proliferation arrest
(PubMed:27556504). Isoform 2 interacts with 14-3-3 proteins
(PubMed:25588844). Isoform 2 interacts (via phosphorylated form)
with YWHAB; this interaction occurs in a chemokine-dependent
manner and does not compete for binding of RIPOR2 with RHOA nor
blocks inhibition of RIPOR2-mediated RHOA activity
(PubMed:25588844). Isoform 2 interacts with YWHAE
(PubMed:25588844). Isoform 2 interacts with YWHAQ
(PubMed:25588844). {ECO:0000250|UniProtKB:Q80U16,
ECO:0000269|PubMed:23241886, ECO:0000269|PubMed:24687993,
ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27556504}.
-!- INTERACTION:
P61586:RHOA; NbExp=4; IntAct=EBI-2798942, EBI-446668;
P08134:RHOC; NbExp=5; IntAct=EBI-2798942, EBI-747589;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17150207,
ECO:0000269|PubMed:23241886}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:17150207}. Cell projection, filopodium
{ECO:0000269|PubMed:17150207}. Cell projection, stereocilium
{ECO:0000250|UniProtKB:Q80U16}. Cell projection, stereocilium
membrane {ECO:0000250|UniProtKB:Q7TP54}. Apical cell membrane
{ECO:0000250|UniProtKB:Q7TP54}. Note=Localized in the cytoplasm in
cells undergoing mitosis (PubMed:17150207). Colocalized with F-
actin (PubMed:17150207). Localized with RHOC within the basal
domain of hair cell stereocilia, near the taper region (By
similarity). Detected in punctate pattern forming a
circumferential ring at the stereocilia base (By similarity).
Localized to the apical stereocilia of inner and outer hair cells
(By similarity). Not detected as a membrane-associated protein in
stereocilia (By similarity). {ECO:0000250|UniProtKB:Q7TP54,
ECO:0000250|UniProtKB:Q80U16, ECO:0000269|PubMed:17150207}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:24687993}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:25588844}. Note=Accumulates at the leading
edge of polarized neutrophils in a chemokine-dependent manner
(PubMed:25588844). {ECO:0000269|PubMed:25588844}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y4F9-1; Sequence=Displayed;
Name=2; Synonyms=PL48 {ECO:0000303|PubMed:9055809};
IsoId=Q9Y4F9-2; Sequence=VSP_025904, VSP_025905, VSP_025906;
-!- TISSUE SPECIFICITY: Expressed in primary fetal mononuclear
myoblast (PubMed:17150207). Expressed strongly in naive T
lymphocytes (PubMed:27556504). Expressed weakly in activated T
lymphocytes (at protein level) (PubMed:27556504). Expressed in
blood cells and adult tissues of hematopoietic origin, such as the
secondary lymphoid organs (PubMed:23241886). Expressed in
cytotrophoblast (PubMed:9055809). {ECO:0000269|PubMed:17150207,
ECO:0000269|PubMed:23241886, ECO:0000269|PubMed:27556504,
ECO:0000269|PubMed:9055809}.
-!- INDUCTION: Up-regulated during fetal mononuclear myoblast
differentiation (PubMed:17150207, PubMed:24687993). Up-regulated
during cytotrophoblast differentiation (PubMed:9055809). Up-
regulated during granulocyte differentiation (PubMed:9055809).
Isoform 1 and isoform 2 are down-regulated in T lymphocytes upon
T-cell antigen receptor (TCR) stimulation (PubMed:27556504).
Isoform 1 and isoform 2 are up-regulated by FOXO1
(PubMed:23241886). {ECO:0000269|PubMed:17150207,
ECO:0000269|PubMed:23241886, ECO:0000269|PubMed:24687993,
ECO:0000269|PubMed:27556504, ECO:0000269|PubMed:9055809}.
-!- PTM: Phosphorylated. Isoform 2 is phosphorylated in T cells
(PubMed:27556504). Chemokine-induced phosphorylation of isoform 2
in neutrophils occurs in a PKC- and AKT-dependent manner,
resulting in RIPOR2 interaction with YWHAB and stabilization
(PubMed:25588844). Isoform 2 is phosphorylated by PKCA, AKT1 and
MAPKAPK1A; in vitro (PubMed:25588844).
{ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27556504}.
-!- PTM: Asn-41 was reported to be N-glycosylated; however as this
position is probably not extracellular, the in vivo relevance is
not proven (PubMed:16335952). Acetylated during myogenic
differentiation (PubMed:24687993). {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:24687993}.
-!- DISEASE: Deafness, autosomal recessive, 104 (DFNB104)
[MIM:616515]: A form of non-syndromic sensorineural hearing loss.
Sensorineural deafness results from damage to the neural receptors
of the inner ear, the nerve pathways to the brain, or the area of
the brain that receives sound information.
{ECO:0000269|PubMed:24958875}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Cells lacking isoform 2 exhibit a severe reduction
of myotube formation. In contrast, isoform 2 overexpression
induces formation of filopodia.
-!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC51134.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=BAA20840.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U49187; AAC51134.1; ALT_FRAME; mRNA.
EMBL; AB002384; BAA20840.2; ALT_INIT; mRNA.
EMBL; AL512428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL078584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471087; EAW55470.1; -; Genomic_DNA.
EMBL; BC001232; AAH01232.1; -; mRNA.
CCDS; CCDS47383.1; -. [Q9Y4F9-1]
CCDS; CCDS47384.1; -. [Q9Y4F9-2]
RefSeq; NP_001273375.1; NM_001286446.2.
RefSeq; NP_001273376.1; NM_001286447.1.
RefSeq; NP_055537.2; NM_014722.4. [Q9Y4F9-1]
RefSeq; NP_056948.2; NM_015864.3. [Q9Y4F9-2]
RefSeq; XP_016867015.1; XM_017011526.1. [Q9Y4F9-2]
RefSeq; XP_016867016.1; XM_017011527.1. [Q9Y4F9-2]
UniGene; Hs.559459; -.
UniGene; Hs.737906; -.
ProteinModelPortal; Q9Y4F9; -.
SMR; Q9Y4F9; -.
BioGrid; 115098; 9.
IntAct; Q9Y4F9; 10.
STRING; 9606.ENSP00000259698; -.
iPTMnet; Q9Y4F9; -.
PhosphoSitePlus; Q9Y4F9; -.
BioMuta; FAM65B; -.
DMDM; 296439477; -.
EPD; Q9Y4F9; -.
PaxDb; Q9Y4F9; -.
PeptideAtlas; Q9Y4F9; -.
PRIDE; Q9Y4F9; -.
DNASU; 9750; -.
Ensembl; ENST00000259698; ENSP00000259698; ENSG00000111913. [Q9Y4F9-1]
Ensembl; ENST00000378023; ENSP00000367262; ENSG00000111913. [Q9Y4F9-2]
Ensembl; ENST00000613507; ENSP00000482957; ENSG00000111913. [Q9Y4F9-1]
GeneID; 9750; -.
KEGG; hsa:9750; -.
UCSC; uc003neo.3; human. [Q9Y4F9-1]
CTD; 9750; -.
DisGeNET; 9750; -.
EuPathDB; HostDB:ENSG00000111913.15; -.
GeneCards; RIPOR2; -.
H-InvDB; HIX0005630; -.
HGNC; HGNC:13872; RIPOR2.
MalaCards; RIPOR2; -.
MIM; 611410; gene.
MIM; 616515; phenotype.
neXtProt; NX_Q9Y4F9; -.
OpenTargets; ENSG00000111913; -.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKB; PA162387677; -.
eggNOG; ENOG410IEN6; Eukaryota.
eggNOG; ENOG410XR7R; LUCA.
GeneTree; ENSGT00490000043360; -.
HOGENOM; HOG000112476; -.
HOVERGEN; HBG053834; -.
InParanoid; Q9Y4F9; -.
OMA; HFREKAL; -.
OrthoDB; EOG091G018M; -.
PhylomeDB; Q9Y4F9; -.
TreeFam; TF329332; -.
ChiTaRS; FAM65B; human.
GenomeRNAi; 9750; -.
PRO; PR:Q9Y4F9; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000111913; -.
CleanEx; HS_FAM65B; -.
ExpressionAtlas; Q9Y4F9; baseline and differential.
Genevisible; Q9Y4F9; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:1990869; P:cellular response to chemokine; IDA:UniProtKB.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0007162; P:negative regulation of cell adhesion; IMP:UniProtKB.
GO; GO:1903904; P:negative regulation of establishment of T cell polarity; IMP:UniProtKB.
GO; GO:1905872; P:negative regulation of protein localization to cell leading edge; ISS:UniProtKB.
GO; GO:2001107; P:negative regulation of Rho guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
GO; GO:2000405; P:negative regulation of T cell migration; IMP:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IMP:UniProtKB.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:UniProtKB.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:2000391; P:positive regulation of neutrophil extravasation; ISS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0048741; P:skeletal muscle fiber development; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR031780; FAM65_N.
InterPro; IPR033035; FAM65B.
InterPro; IPR026136; RIPOR3.
PANTHER; PTHR15829; PTHR15829; 1.
PANTHER; PTHR15829:SF2; PTHR15829:SF2; 1.
Pfam; PF15903; PL48; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
Chemotaxis; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Deafness; Developmental protein; Differentiation; Hearing; Membrane;
Myogenesis; Non-syndromic deafness; Phosphoprotein; Polymorphism;
Reference proteome; Signal transduction inhibitor.
CHAIN 1 1068 Rho family-interacting cell polarization
regulator 2.
/FTId=PRO_0000289114.
REGION 55 113 Involved in cell filopodia formation.
{ECO:0000269|PubMed:17150207}.
COILED 83 112 {ECO:0000255}.
COILED 768 793 {ECO:0000255}.
MOD_RES 21 21 Phosphoserine; in isoform 2.
{ECO:0000269|PubMed:25588844}.
MOD_RES 37 37 Phosphoserine; in isoform 2.
{ECO:0000269|PubMed:25588844}.
MOD_RES 341 341 Phosphoserine; in isoform 2.
{ECO:0000269|PubMed:25588844}.
MOD_RES 523 523 Phosphoserine; in isoform 2.
{ECO:0000269|PubMed:25588844}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000250|UniProtKB:Q80U16}.
MOD_RES 585 585 Phosphoserine; in isoform 2.
{ECO:0000269|PubMed:25588844}.
VAR_SEQ 360 409 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9055809}.
/FTId=VSP_025904.
VAR_SEQ 641 641 C -> K (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9055809}.
/FTId=VSP_025905.
VAR_SEQ 642 1068 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9055809}.
/FTId=VSP_025906.
VARIANT 145 145 A -> G (in dbSNP:rs11967003).
/FTId=VAR_032572.
VARIANT 320 320 V -> M (in dbSNP:rs35331811).
{ECO:0000269|PubMed:9205841}.
/FTId=VAR_032573.
VARIANT 424 424 E -> K (in dbSNP:rs34016544).
/FTId=VAR_032574.
VARIANT 452 452 S -> C (in dbSNP:rs34298086).
/FTId=VAR_032575.
VARIANT 495 495 E -> K (in dbSNP:rs35514577).
/FTId=VAR_032576.
VARIANT 520 520 R -> C (in dbSNP:rs35780910).
/FTId=VAR_032577.
VARIANT 868 868 R -> Q (in dbSNP:rs9461073).
{ECO:0000269|PubMed:9205841}.
/FTId=VAR_062193.
MUTAGEN 21 21 S->A: Reduces phosphorylation,
interaction with HDAC6, YWHAB and 14-3-3
proteins, localization at the front of
the neutrophil upon chemokine stimulation
and prevents T cell proliferation
inhibition; when associated with A-37; A-
341; A-523 and A-585 (isoform 2).
{ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27556504}.
MUTAGEN 37 37 S->A: Reduces phosphorylation,
interaction with HDAC6, YWHAB and 14-3-3
proteins, localization at the front of
the neutrophil upon chemokine stimulation
and prevents T cell proliferation
inhibition; when associated with A-21; A-
341; A-523 and A-585 (isoform 2).
{ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27556504}.
MUTAGEN 151 152 RL->AA: Inhibits interaction with RHOA
and does not prevent T cell proliferation
inhibition; in isoform 2.
{ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27556504}.
MUTAGEN 155 156 GA->RR: Inhibits interaction with RHOA;
in isoform 2.
{ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27556504}.
MUTAGEN 341 341 S->A: Reduces phosphorylation,
interaction with HDAC6, YWHAB and 14-3-3
proteins, localization at the front of
the neutrophil upon chemokine stimulation
and prevents T cell proliferation
inhibition; when associated with A-21; A-
37; A-523 and A-585 (isoform 2).
{ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27556504}.
MUTAGEN 523 523 S->A: Reduces phosphorylation,
interaction with HDAC6, YWHAB and 14-3-3
proteins, localization at the front of
the neutrophil upon chemokine stimulation
and prevents T cell proliferation
inhibition; when associated with A-21; A-
37; A-341 and A-585 (isoform 2).
{ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27556504}.
MUTAGEN 585 585 S->A: Reduces phosphorylation,
interaction with HDAC6, YWHAB and 14-3-3
proteins, localization at the front of
the neutrophil upon chemokine stimulation
and prevents T cell proliferation
inhibition; when associated with A-21; A-
37; A-341 and A-523 (isoform 2).
{ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27556504}.
CONFLICT 13 13 P -> A (in Ref. 1; AAC51134).
{ECO:0000305}.
SEQUENCE 1068 AA; 118519 MW; CCA7DEB3A66F36AA CRC64;
MLVGSQSFSP GGPNGIIRSQ SFAGFSGLQE RRSRCNSFIE NSSALKKPQA KLKKMHNLGH
KNNNPPKEPQ PKRVEEVYRA LKNGLDEYLE VHQTELDKLT AQLKDMKRNS RLGVLYDLDK
QIKTIERYMR RLEFHISKVD ELYEAYCIQR RLQDGASKMK QAFATSPASK AARESLTEIN
RSFKEYTENM CTIEVELENL LGEFSIKMKG LAGFARLCPG DQYEIFMKYG RQRWKLKGKI
EVNGKQSWDG EETVFLPLIV GFISIKVTEL KGLATHILVG SVTCETKELF AARPQVVAVD
INDLGTIKLN LEITWYPFDV EDMTASSGAG NKAAALQRRM SMYSQGTPET PTFKDHSFFR
WLHPSPDKPR RLSVLSALQD TFFAKLHRSR SFSDLPSLRP SPKAVLELYS NLPDDIFENG
KAAEEKMPLS LSFSDLPNGD CALTSHSTGS PSNSTNPEIT ITPAEFNLSS LASQNEGMDD
TSSASSRNSL GEGQEPKSHL KEEDPEEPRK PASAPSEACR RQSSGAGAEH LFLENDVAEA
LLQESEEASE LKPVELDTSE GNITKQLVKR LTSAEVPMAT DRLLSEGSVG GESEGCRSFL
DGSLEDAFNG LLLALEPHKE QYKEFQDLNQ EVMNLDDILK CKPAVSRSRS SSLSLTVESA
LESFDFLNTS DFDEEEDGDE VCNVGGGADS VFSDTETEKH SYRSVHPEAR GHLSEALTED
TGVGTSVAGS PLPLTTGNES LDITIVRHLQ YCTQLVQQIV FSSKTPFVAR SLLEKLSRQI
QVMEKLAAVS DENIGNISSV VEAIPEFHKK LSLLSFWTKC CSPVGVYHSP ADRVMKQLEA
SFARTVNKEY PGLADPVFRT LVSQILDRAE PLLSSSLSSE VVTVFQYYSY FTSHGVSDLE
SYLSQLARQV SMVQTLQSLR DEKLLQTMSD LAPSNLLAQQ EVLRTLALLL TREDNEVSEA
VTLYLAAASK NQHFREKALL YYCEALTKTN LQLQKAACLA LKILEATESI KMLVTLCQSD
TEEIRNVASE TLLSLGEDGR LAYEQLDKFP RDCVKVGGRH GTEVATAF


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