ID   MELT_RAT                Reviewed;         832 AA.
AC   Q5PQS3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Ventricular zone-expressed PH domain-containing protein homolog 1;
DE   AltName: Full=Protein melted homolog;
GN   Name=Veph1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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).
CC   -!- FUNCTION: Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits
CC       dissociation of activated SMAD2 from TGFBR1, impeding its nuclear
CC       accumulation and resulting in impaired TGF-beta signaling. May also
CC       affect FOXO, Hippo and Wnt signaling. {ECO:0000250|UniProtKB:Q14D04}.
CC   -!- SUBUNIT: Interacts with TGFBR1. {ECO:0000250|UniProtKB:Q14D04}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14D04};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q9VS24}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:Q9VS24}.
CC   -!- DOMAIN: The PH domain is required for membrane targeting.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MELT/VEPH family. {ECO:0000305}.
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DR   EMBL; BC087055; AAH87055.1; -; mRNA.
DR   RefSeq; NP_001014193.1; NM_001014171.1.
DR   AlphaFoldDB; Q5PQS3; -.
DR   STRING; 10116.ENSRNOP00000016621; -.
DR   iPTMnet; Q5PQS3; -.
DR   PhosphoSitePlus; Q5PQS3; -.
DR   PaxDb; Q5PQS3; -.
DR   PRIDE; Q5PQS3; -.
DR   Ensembl; ENSRNOT00000016621; ENSRNOP00000016621; ENSRNOG00000012427.
DR   GeneID; 361954; -.
DR   KEGG; rno:361954; -.
DR   UCSC; RGD:1308217; rat.
DR   CTD; 79674; -.
DR   RGD; 1308217; Veph1.
DR   eggNOG; KOG3723; Eukaryota.
DR   GeneTree; ENSGT00390000018660; -.
DR   InParanoid; Q5PQS3; -.
DR   PhylomeDB; Q5PQS3; -.
DR   TreeFam; TF314736; -.
DR   PRO; PR:Q5PQS3; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000012427; Expressed in heart and 9 other tissues.
DR   ExpressionAtlas; Q5PQS3; baseline and differential.
DR   Genevisible; Q5PQS3; RN.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IBA:GO_Central.
DR   GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039888; Melted-like.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR21630; PTHR21630; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome.
FT   CHAIN           1..832
FT                   /note="Ventricular zone-expressed PH domain-containing
FT                   protein homolog 1"
FT                   /id="PRO_0000297957"
FT   DOMAIN          716..818
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          201..319
FT                   /note="Interaction with TGFBR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q14D04"
FT   REGION          497..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..832
FT                   /note="Interaction with TGFBR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q14D04"
FT   COMPBIAS        498..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  94463 MW;  E29E5FFB6DAF1404 CRC64;
     MHQLFRLVLG QKDLSRAGDL FSLDDAEIED SLTEALEQIK VISSSLDYQT NNNDQAVVEI
     CITRITTAIR ETESIEKHAR ALVGLWDSCL EHNLRPAGKD EDTPHAKIAS DIMSCILQNY
     NRTPVMVLAV PIAVKFLHRG SKELCRNMSN YLSLAAITKA DLLADHTEGI VKSILQGNAM
     LLRVLPAVYE KQPQPINRHL AELLALMSQL EQTEQYHLLR LLHVAAKRKD VEVVQKCVPF
     LIRNLKESTY NDIILNILIE IAGHEPLALN SFLPMLKEIA EQFPYLTGQM ARIFGAVGHV
     DEERARSCLR YLVSQLANME HSFHHILLLE IKSLTDAFSS ILGPHSRDIF RMSNSFTNIA
     KLLSRQLENS KAESGRRRTG TEVSFPEKFR EPKTMEPKSE DHEKLQVKIQ AFEDKINAES
     HTPGSVRRYS LDHVSKEERK NVRFSRSRSL ALNTVLTNSV NVEDGEIEGK TGMHASISLS
     EIDPPGHGIG KVPFKTDTHG SQLRNSSASH PSIIHSEPEN MPETFKENVQ EEIPEAAISP
     VEYQDKLYLH LKENLSKVKA YALEIAKKVP IPDQCTIEDN TRSCVAKLFF TCSLKGHYCL
     YSKSSFTLVS QAPQPWIQIM FLFQQSLFPE PLSIQSGSVQ FLKALWEKTQ GTGTHSFEVA
     MTESTFPQQK DLDQLQLHLE EVRFFDVFGF SETAGAWQCF MCNNPEKATV INQDGQPLIE
     GKLKEKQVRW KFIKRWKTRY FTLAGNQLLF QKGKSDDPDD SPIELSKVQS VKAVAKKRRD
     RSLPRAFEIF TDNKTYVFKA KDEKNAEEWL QCINVALAQA KERESREVTT YL