ID   RHPN2_BOVIN             Reviewed;         686 AA.
AC   A4FUC9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Rhophilin-2;
DE   AltName: Full=GTP-Rho-binding protein 2;
GN   Name=RHPN2;
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the RHPN family. {ECO:0000305}.
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DR   EMBL; BC114709; AAI14710.1; -; mRNA.
DR   RefSeq; NP_001076939.1; NM_001083470.1.
DR   AlphaFoldDB; A4FUC9; -.
DR   SMR; A4FUC9; -.
DR   STRING; 9913.ENSBTAP00000004021; -.
DR   PaxDb; A4FUC9; -.
DR   PRIDE; A4FUC9; -.
DR   Ensembl; ENSBTAT00000004021; ENSBTAP00000004021; ENSBTAG00000003089.
DR   GeneID; 533687; -.
DR   KEGG; bta:533687; -.
DR   CTD; 85415; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003089; -.
DR   VGNC; VGNC:52240; RHPN2.
DR   eggNOG; KOG2220; Eukaryota.
DR   GeneTree; ENSGT00940000153837; -.
DR   InParanoid; A4FUC9; -.
DR   OMA; MICLAYD; -.
DR   OrthoDB; 641122at2759; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000003089; Expressed in saliva-secreting gland and 99 other tissues.
DR   ExpressionAtlas; A4FUC9; baseline and differential.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
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_0000340662"
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;  77105 MW;  1BA093658287DE96 CRC64;
     MTDTLLPAAP QPLEKEGNCY FRKGCNPLAQ TGRSKLQNQR AALNQQILKA MRMRTGAENL
     LKAATNQKVR EQVRLELSFL NSDLQMLKEE LEGLNISVGV YQNTEEAFTI PLIPLGLKET
     KDVDFSVALK DFILEHYSED SYLYEDEIAD LMDLRQACRT PSRNEAGVEL LMSYFMQLGF
     VESRFFPPTR QMGILFTWYD SLTGVPVSQQ NLLLEKASIL FNIGALYTQI GTRCNRQTEA
     GLESTVDAFQ RAAGVLNYLK ETFTHTPSYD MSPAMLSVLV KMMLAQAQES TFEKVCLPGL
     QNEFFLLVKV AQEAAKVGEV YRQLHTAMNQ EPVKENIPYS WASLACVKAH HYEALAHYFT
     ATLLIDHQLK PGEDEDHQEK CLSQLYSHMP EGLTPLATLK NVHQRQLLGK SHLCQAVTHH
     EESMREASLC KKLRNIDVLQ EVLSAAHDRS QLKYTQLRED DDLLNLTDAP DIVSKTEREV
     EIIVPQFSKV TVTDFFQKLG PLSVFSANKR WTAPRSIHFT AEEGDLGFTL RGNSPVQVHF
     LDPYCSAAAA GTKEGDYIVS IQDVDCKWLT LSEVMKMLKS FGQDDIEMKV VSLLDATSTM
     HSKCATYSVG MQKTYSMICL GIDVDDKTDK TKKVSKKLSF LSWGTNKNRQ KSASTLCLPS
     VGVTMPPVKK KLSSPFSLLN TDSSLY