RHPN1_HUMAN
ID RHPN1_HUMAN Reviewed; 670 AA.
AC Q8TCX5; Q8TAV1; Q96PV9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Rhophilin-1 {ECO:0000305};
DE AltName: Full=GTP-Rho-binding protein 1;
GN Name=RHPN1 {ECO:0000312|HGNC:HGNC:19973}; Synonyms=KIAA1929;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Burbelo P.D.;
RT "Structure and function of rhophilin homologs.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-670.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
CC -!- FUNCTION: Has no enzymatic activity. May serve as a target for Rho, and
CC interact with some cytoskeletal component upon Rho binding or relay a
CC Rho signal to other molecules. {ECO:0000250|UniProtKB:Q61085}.
CC -!- SUBUNIT: Binds specifically to GTP-Rho. Interacts with ROPN1.
CC {ECO:0000250|UniProtKB:Q61085}.
CC -!- INTERACTION:
CC Q8TCX5; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-746325, EBI-739624;
CC Q8TCX5; P14136: GFAP; NbExp=3; IntAct=EBI-746325, EBI-744302;
CC Q8TCX5; Q08379: GOLGA2; NbExp=4; IntAct=EBI-746325, EBI-618309;
CC Q8TCX5; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-746325, EBI-473189;
CC Q8TCX5; P28799: GRN; NbExp=3; IntAct=EBI-746325, EBI-747754;
CC Q8TCX5; P54257: HAP1; NbExp=3; IntAct=EBI-746325, EBI-712814;
CC Q8TCX5; Q15323: KRT31; NbExp=3; IntAct=EBI-746325, EBI-948001;
CC Q8TCX5; P02545: LMNA; NbExp=3; IntAct=EBI-746325, EBI-351935;
CC Q8TCX5; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-746325, EBI-1216080;
CC Q8TCX5; Q5JR59: MTUS2; NbExp=4; IntAct=EBI-746325, EBI-742948;
CC Q8TCX5; P07196: NEFL; NbExp=3; IntAct=EBI-746325, EBI-475646;
CC Q8TCX5; O43933: PEX1; NbExp=3; IntAct=EBI-746325, EBI-988601;
CC Q8TCX5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-746325, EBI-5235340;
CC Q8TCX5; P14373: TRIM27; NbExp=3; IntAct=EBI-746325, EBI-719493;
CC Q8TCX5; O76024: WFS1; NbExp=3; IntAct=EBI-746325, EBI-720609;
CC -!- DOMAIN: The PDZ domain mediates interaction with ROPN1.
CC {ECO:0000250|UniProtKB:Q61085}.
CC -!- SIMILARITY: Belongs to the RHPN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL89809.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAB67822.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB67822.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY082588; AAL89809.1; ALT_SEQ; mRNA.
DR EMBL; BC025767; AAH25767.1; -; mRNA.
DR EMBL; AB067516; BAB67822.1; ALT_SEQ; mRNA.
DR CCDS; CCDS47927.1; -.
DR RefSeq; NP_443156.2; NM_052924.2.
DR AlphaFoldDB; Q8TCX5; -.
DR SMR; Q8TCX5; -.
DR BioGRID; 125372; 52.
DR IntAct; Q8TCX5; 52.
DR STRING; 9606.ENSP00000289013; -.
DR iPTMnet; Q8TCX5; -.
DR PhosphoSitePlus; Q8TCX5; -.
DR BioMuta; RHPN1; -.
DR DMDM; 30173334; -.
DR EPD; Q8TCX5; -.
DR jPOST; Q8TCX5; -.
DR MassIVE; Q8TCX5; -.
DR PaxDb; Q8TCX5; -.
DR PeptideAtlas; Q8TCX5; -.
DR PRIDE; Q8TCX5; -.
DR Antibodypedia; 7394; 169 antibodies from 25 providers.
DR DNASU; 114822; -.
DR Ensembl; ENST00000289013.11; ENSP00000289013.6; ENSG00000158106.14.
DR GeneID; 114822; -.
DR KEGG; hsa:114822; -.
DR MANE-Select; ENST00000289013.11; ENSP00000289013.6; NM_052924.3; NP_443156.2.
DR UCSC; uc003yyb.4; human.
DR CTD; 114822; -.
DR DisGeNET; 114822; -.
DR GeneCards; RHPN1; -.
DR HGNC; HGNC:19973; RHPN1.
DR HPA; ENSG00000158106; Tissue enhanced (pituitary gland, thyroid gland).
DR MIM; 601031; gene.
DR neXtProt; NX_Q8TCX5; -.
DR OpenTargets; ENSG00000158106; -.
DR PharmGKB; PA134987144; -.
DR VEuPathDB; HostDB:ENSG00000158106; -.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT00940000153837; -.
DR HOGENOM; CLU_006514_3_0_1; -.
DR InParanoid; Q8TCX5; -.
DR OMA; THPDFGQ; -.
DR OrthoDB; 641122at2759; -.
DR PhylomeDB; Q8TCX5; -.
DR TreeFam; TF323502; -.
DR PathwayCommons; Q8TCX5; -.
DR Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q8TCX5; -.
DR BioGRID-ORCS; 114822; 73 hits in 1072 CRISPR screens.
DR GeneWiki; RHPN1; -.
DR GenomeRNAi; 114822; -.
DR Pharos; Q8TCX5; Tbio.
DR PRO; PR:Q8TCX5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8TCX5; protein.
DR Bgee; ENSG00000158106; Expressed in right lobe of thyroid gland and 148 other tissues.
DR Genevisible; Q8TCX5; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09248; BRO1_Rhophilin_1; 1.
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 InterPro; IPR042715; Rhophilin-1_BRO1.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF02185; HR1; 1.
DR Pfam; PF00595; PDZ; 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 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..670
FT /note="Rhophilin-1"
FT /id="PRO_0000218895"
FT DOMAIN 23..97
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 108..457
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT DOMAIN 513..592
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..670
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61085"
SQ SEQUENCE 670 AA; 73590 MW; CE8C01B716465FF0 CRC64;
MILEERPDGA GAGEESPRLQ GCDSLTQIQC GQLQSRRAQI HQQIDKELQM RTGAENLYRA
TSNNRVRETV ALELSYVNSN LQLLKEELEE LSGGVDPGRH GSEAVTVPMI PLGLKETKEL
DWSTPLKELI SVHFGEDGAS YEAEIRELEA LRQAMRTPSR NESGLELLTA YYNQLCFLDA
RFLTPARSLG LFFHWYDSLT GVPAQQRALA FEKGSVLFNI GALHTQIGAR QDRSCTEGAR
RAMEAFQRAA GAFSLLRENF SHAPSPDMSA ASLCALEQLM MAQAQECVFE GLSPPASMAP
QDCLAQLRLA QEAAQVAAEY RLVHRTMAQP PVHDYVPVSW TALVHVKAEY FRSLAHYHVA
MALCDGSPAT EGELPTHEQV FLQPPTSSKP RGPVLPQELE ERRQLGKAHL KRAILGQEEA
LRLHALCRVL REVDLLRAVI SQTLQRSLAK YAELDREDDF CEAAEAPDIQ PKTHQKPEAR
MPRLSQGKGP DIFHRLGPLS VFSAKNRWRL VGPVHLTRGE GGFGLTLRGD SPVLIAAVIP
GSQAAAAGLK EGDYIVSVNG QPCRWWRHAE VVTELKAAGE AGASLQVVSL LPSSRLPSLG
DRRPVLLGPR GLLRSQREHG CKTPASTWAS PRPLLNWSRK AQQGKTGGCP QPCAPVKPAP
PSSLKHPGWP
