ID VMP1_HUMAN Reviewed; 406 AA. AC Q96GC9; Q9H0P4; Q9P089; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 18-APR-2012, entry version 75. DE RecName: Full=Vacuole membrane protein 1; DE AltName: Full=Transmembrane protein 49; GN Name=VMP1; Synonyms=TDC1, TMEM49; ORFNames=HSPC292; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wu G., Couch F.J.; RT "Gene Tdc1 is a transmembrane domain containing gene that amplified RT and overexpressed in human breast cancer."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Yamazaki S., Muta T., Takeshige K.; RT "A novel lipopolysaccharide-inducible gene (#25)."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-406. RC TISSUE=Blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, INTERACTION WITH TJP1, AND SUBCELLULAR LOCATION. RX PubMed=17724469; DOI=10.1038/sj.onc.1210743; RA Sauermann M., Sahin O., Sultmann H., Hahne F., Blaszkiewicz S., RA Majety M., Zatloukal K., Fuzesi L., Poustka A., Wiemann S., Arlt D.; RT "Reduced expression of vacuole membrane protein 1 affects the invasion RT capacity of tumor cells."; RL Oncogene 27:1320-1326(2008). CC -!- FUNCTION: Stress-induced protein that, when overexpressed, CC promotes formation of intracellular vacuoles followed by cell CC death. May be involved in the cytoplasmic vacuolization of acinar CC cells during the early stage of acute pancreatitis. Plays a role CC in the initial stages of the autophagic process through its CC interaction with BECN1 (By similarity). Involved in cell-cell CC adhesion. Plays an essential role in formation of cell junctions. CC -!- SUBUNIT: Interacts with BECN1. Interacts with TJP1. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate CC compartment membrane; Multi-pass membrane protein (By similarity). CC Cell membrane; Multi-pass membrane protein. Vacuole membrane; CC Multi-pass membrane protein (By similarity). Endoplasmic CC reticulum. CC -!- SIMILARITY: Belongs to the VMP1 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF214006; AAL36461.1; -; mRNA. DR EMBL; AB047551; BAF47368.1; -; mRNA. DR EMBL; AL136711; CAB66646.1; -; mRNA. DR EMBL; CR533521; CAG38552.1; -; mRNA. DR EMBL; BC009758; AAH09758.1; -; mRNA. DR EMBL; AF161410; AAF28970.1; -; mRNA. DR IPI; IPI00792839; -. DR RefSeq; NP_112200.2; NM_030938.3. DR UniGene; Hs.444569; -. DR UniGene; Hs.708260; -. DR ProteinModelPortal; Q96GC9; -. DR IntAct; Q96GC9; 3. DR STRING; Q96GC9; -. DR PhosphoSite; Q96GC9; -. DR DMDM; 74731809; -. DR PRIDE; Q96GC9; -. DR DNASU; 81671; -. DR Ensembl; ENST00000262291; ENSP00000262291; ENSG00000062716. DR GeneID; 81671; -. DR KEGG; hsa:81671; -. DR UCSC; uc002ixu.4; human. DR CTD; 81671; -. DR GeneCards; GC17P057785; -. DR HGNC; HGNC:29559; VMP1. DR HPA; HPA030773; -. DR MIM; 611753; gene. DR neXtProt; NX_Q96GC9; -. DR PharmGKB; PA142670765; -. DR eggNOG; NOG321939; -. DR GeneTree; ENSGT00390000007230; -. DR HOGENOM; HBG591351; -. DR HOVERGEN; HBG057290; -. DR InParanoid; Q96GC9; -. DR OMA; XIPNPLF; -. DR OrthoDB; EOG4K0QNM; -. DR PhylomeDB; Q96GC9; -. DR NextBio; 72028; -. DR ArrayExpress; Q96GC9; -. DR Bgee; Q96GC9; -. DR CleanEx; HS_TMEM49; -. DR Genevestigator; Q96GC9; -. DR GO; GO:0000421; C:autophagic vacuole membrane; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB. DR GO; GO:0016337; P:cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB. PE 1: Evidence at protein level; KW Autophagy; Cell adhesion; Cell membrane; Complete proteome; KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Vacuole. FT CHAIN 1 406 Vacuole membrane protein 1. FT /FTId=PRO_0000284546. FT TOPO_DOM 1 43 Cytoplasmic (Potential). FT TRANSMEM 44 64 Helical; (Potential). FT TOPO_DOM 65 77 Extracellular (Potential). FT TRANSMEM 78 98 Helical; (Potential). FT TOPO_DOM 99 109 Cytoplasmic (Potential). FT TRANSMEM 110 130 Helical; (Potential). FT TOPO_DOM 131 250 Extracellular (Potential). FT TRANSMEM 251 271 Helical; (Potential). FT TOPO_DOM 272 273 Cytoplasmic (Potential). FT TRANSMEM 274 294 Helical; (Potential). FT TOPO_DOM 295 305 Extracellular (Potential). FT TRANSMEM 306 326 Helical; (Potential). FT TOPO_DOM 327 363 Cytoplasmic (Potential). FT TRANSMEM 364 384 Helical; (Potential). FT TOPO_DOM 385 406 Extracellular (Potential). FT CONFLICT 179 179 S -> F (in Ref. 3; CAB66646 and 4; FT CAG38552). SQ SEQUENCE 406 AA; 46238 MW; E9DDE63F80143091 CRC64; MAENGKNCDQ RRVAMNKEHH NGNFTDPSSV NEKKRREREE RQNIVLWRQP LITLQYFSLE ILVILKEWTS KLWHRQSIVV SFLLLLAVLI ATYYVEGVHQ QYVQRIEKQF LLYAYWIGLG ILSSVGLGTG LHTFLLYLGP HIASVTLAAY ECNSVNFPEP PYPDQIICPD EEGTEGTISL WSIISKVRIE ACMWGIGTAI GELPPYFMAR AARLSGAEPD DEEYQEFEEM LEHAESAQDF ASRAKLAVQK LVQKVGFFGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK MHIQKIFVII TFSKHIVEQM VAFIGAVPGI GPSLQKPFQE YLEAQRQKLH HKSEMGTPQG ENWLSWMFEK LVVVMVCYFI LSIINSMAQS YAKRIQQRLN SEEKTK //