ID   RHPN2_CANLF             Reviewed;         686 AA.
AC   Q8HXG3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Rhophilin-2;
DE   AltName: Full=76 kDa RhoB effector protein;
DE   AltName: Full=GTP-Rho-binding protein 2;
DE   AltName: Full=p76RBE;
GN   Name=RHPN2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=12473120; DOI=10.1046/j.1432-1033.2002.03343.x;
RA   Mircescu H., Steuve S., Savonet V., Degraef C., Mellor H., Dumont J.E.,
RA   Maenhaut C., Pirson I.;
RT   "Identification and characterization of a novel activated RhoB binding
RT   protein containing a PDZ domain whose expression is specifically modulated
RT   in thyroid cells by cAMP.";
RL   Eur. J. Biochem. 269:6241-6249(2002).
RN   [2]
RP   IDENTIFICATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=8910471; DOI=10.1074/jbc.271.45.28451;
RA   Wilkin F., Savonet V., Radulescu A., Petermans J., Dumont J.E.,
RA   Maenhaut C.;
RT   "Identification and characterization of novel genes modulated in the
RT   thyroid of dogs treated with methimazole and propylthiouracil.";
RL   J. Biol. Chem. 271:28451-28457(1996).
CC   -!- FUNCTION: Binds specifically to GTP-Rho. May function in a Rho pathway
CC       to limit stress fiber formation and/or increase the turnover of F-actin
CC       structures in the absence of high levels of RhoA activity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GTP-bound RhoA and RhoB. Interacts with both
CC       GTP- and GDP-bound RhoA. Interacts with KRT18 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in thyroid.
CC       {ECO:0000269|PubMed:8910471}.
CC   -!- INDUCTION: By thyrotropin (TSH). {ECO:0000269|PubMed:8910471}.
CC   -!- SIMILARITY: Belongs to the RHPN family. {ECO:0000305}.
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DR   EMBL; AJ347749; CAC87938.1; -; mRNA.
DR   RefSeq; NP_001003008.1; NM_001003008.1.
DR   AlphaFoldDB; Q8HXG3; -.
DR   SMR; Q8HXG3; -.
DR   STRING; 9615.ENSCAFP00000011084; -.
DR   PaxDb; Q8HXG3; -.
DR   GeneID; 403518; -.
DR   KEGG; cfa:403518; -.
DR   CTD; 85415; -.
DR   eggNOG; KOG2220; Eukaryota.
DR   InParanoid; Q8HXG3; -.
DR   OrthoDB; 641122at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.25.40.280; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR004328; BRO1_dom.
DR   InterPro; IPR038499; BRO1_sf.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   Pfam; PF03097; BRO1; 1.
DR   Pfam; PF02185; HR1; 1.
DR   SMART; SM01041; BRO1; 1.
DR   SMART; SM00742; Hr1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF46585; SSF46585; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS51180; BRO1; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS51860; REM_1; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..686
FT                   /note="Rhophilin-2"
FT                   /id="PRO_0000218897"
FT   DOMAIN          26..100
FT                   /note="REM-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          111..460
FT                   /note="BRO1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT   DOMAIN          515..593
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          46..66
FT                   /note="Interaction with Rho"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         655
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWR8"
SQ   SEQUENCE   686 AA;  76865 MW;  DA554284E53C4318 CRC64;
     MTDALLPAAP QPLEKESDGY FRKGCNPLAQ TGRSKLQNQR AALNQQILKA VRMRTGAENL
     LKVATNHKVR EQVRLELSFV NSDLQMLKEE LEGLNISVGV YQSTEEAFTV PLIPLGLKET
     KDIDFSVVLK DFILEHYSED SYLYEDEIAD LMDLRQACRT PSRDEAGVEL LMSYFIQLGF
     VESRFFPPTR QMGILFTWYD SLTGVPVSQQ NLLLEKASIL FNIGALYTQI GTRCNRRTQA
     GLDGAVDAFQ RAAGVLHHLK ETFTHTPSYD MSPAMLSVLV KMMLAQAQEN VFEKICLPGI
     RNEFFVLVKV AQEAAKVGEV YRQLHTAMSQ APVKENIPYS WASLVCVKAH HYAALAHYFA
     ATLLIDHQLK PGADEDHQEK CLSQLYDHMP EGLTPLATLK SGHQRRQLGK SHLRRAVAHH
     EESVREASLC KKLRNIEVLQ DVLSVAHERS RLKYAQHQDD DDLLNLIDAP DIISKTEQEV
     EIILPQFSKV TATDFFQKLG PLSVFSANKR WTPPRSIHFT AEEGDLGFTL RGNSPVQVHF
     LDPHCSAALA GAKEGDYIVS IQDVDCKWLT VSEVMKLLKA CGRDGVEMKV VSLLDFTSSM
     HNKCATYSVG MQKTYSMICL AIDDDDKTDK TKKISKKLSF LSWGTDKNRV KSASTLCLPS
     VGVARPQVKK KLPSPFSLLN SDSSLY