EMC10_MOUSE
ID EMC10_MOUSE Reviewed; 258 AA.
AC Q3TAS6; Q3TFU1; Q5UCC3; Q5UCC5; Q8VCD8; Q99JJ8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ER membrane protein complex subunit 10;
DE AltName: Full=Hematopoietic signal peptide-containing membrane domain-containing protein 1;
DE Flags: Precursor;
GN Name=Emc10; Synonyms=Hsm1, Inm02;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=20680400; DOI=10.1007/s11060-010-0314-6;
RA Junes-Gill K.S., Gallaher T.K., Gluzman-Poltorak Z., Miller J.D.,
RA Wheeler C.J., Fan X., Basile L.A.;
RT "hHSS1: a novel secreted factor and suppressor of glioma growth located at
RT chromosome 19q13.33.";
RL J. Neurooncol. 102:197-211(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28931551; DOI=10.1161/circulationaha.117.029980;
RA Reboll M.R., Korf-Klingebiel M., Klede S., Polten F., Brinkmann E.,
RA Reimann I., Schoenfeld H.J., Bobadilla M., Faix J., Kensah G., Gruh I.,
RA Klintschar M., Gaestel M., Niessen H.W., Pich A., Bauersachs J.,
RA Gogos J.A., Wang Y., Wollert K.C.;
RT "EMC10 (endoplasmic reticulum membrane protein complex subunit 10) is a
RT bone marrow-derived angiogenic growth factor promoting tissue repair after
RT myocardial infarction.";
RL Circulation 136:1809-1823(2017).
CC -!- FUNCTION: Part of the endoplasmic reticulum membrane protein complex
CC (EMC) that enables the energy-independent insertion into endoplasmic
CC reticulum membranes of newly synthesized membrane proteins.
CC Preferentially accommodates proteins with transmembrane domains that
CC are weakly hydrophobic or contain destabilizing features such as
CC charged and aromatic residues. Involved in the cotranslational
CC insertion of multi-pass membrane proteins in which stop-transfer
CC membrane-anchor sequences become ER membrane spanning helices. It is
CC also required for the post-translational insertion of tail-anchored/TA
CC proteins in endoplasmic reticulum membranes. By mediating the proper
CC cotranslational insertion of N-terminal transmembrane domains in an N-
CC exo topology, with translocated N-terminus in the lumen of the ER,
CC controls the topology of multi-pass membrane proteins like the G
CC protein-coupled receptors (By similarity). By regulating the insertion
CC of various proteins in membranes, it is indirectly involved in many
CC cellular processes. Promotes angiogenesis and tissue repair in the
CC heart after myocardial infarction. Stimulates cardiac endothelial cell
CC migration and outgrowth via the activation of p38 MAPK, PAK and MAPK2
CC signaling pathways (PubMed:28931551). {ECO:0000250|UniProtKB:Q5UCC4,
CC ECO:0000269|PubMed:28931551}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q5UCC4}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:28931551}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5UCC4}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q5UCC4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TAS6-1; Sequence=Displayed;
CC Name=2; Synonyms=Hematopoietic signal peptide-containing secreted
CC protein 1, HSS1;
CC IsoId=Q3TAS6-2; Sequence=VSP_030475;
CC -!- TISSUE SPECIFICITY: Up-regulated in the left ventricle 3 days after
CC myocardial infarction (MI). Expressed predominantly by monocytes and
CC macrophages from bone marrow, spleen, and peripheral blood 3 days after
CC MI (protein level). {ECO:0000269|PubMed:28931551}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show no cardiovascular phenotype at
CC baseline. After myocardial infarction however, capillarization of the
CC infarct border zone is impaired and the animals develop larger infarct
CC scars and more pronounced left ventricular remodeling and systolic
CC dysfunction compared with wild-type mice.
CC {ECO:0000269|PubMed:28931551}.
CC -!- SIMILARITY: Belongs to the EMC10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE40807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE42592.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY761096; AAV30544.1; -; mRNA.
DR EMBL; AY761098; AAV30546.1; -; mRNA.
DR EMBL; AK169010; BAE40807.1; ALT_INIT; mRNA.
DR EMBL; AK171657; BAE42592.1; ALT_INIT; mRNA.
DR EMBL; BC006065; AAH06065.1; -; mRNA.
DR EMBL; BC020179; AAH20179.1; -; mRNA.
DR CCDS; CCDS52231.2; -. [Q3TAS6-1]
DR RefSeq; NP_932108.2; NM_197991.2. [Q3TAS6-1]
DR AlphaFoldDB; Q3TAS6; -.
DR SMR; Q3TAS6; -.
DR BioGRID; 213613; 2.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR STRING; 10090.ENSMUSP00000008284; -.
DR GlyConnect; 2303; 6 N-Linked glycans (1 site).
DR GlyGen; Q3TAS6; 1 site, 6 N-linked glycans (1 site).
DR PhosphoSitePlus; Q3TAS6; -.
DR EPD; Q3TAS6; -.
DR jPOST; Q3TAS6; -.
DR MaxQB; Q3TAS6; -.
DR PaxDb; Q3TAS6; -.
DR PeptideAtlas; Q3TAS6; -.
DR PRIDE; Q3TAS6; -.
DR ProteomicsDB; 275607; -. [Q3TAS6-1]
DR ProteomicsDB; 275608; -. [Q3TAS6-2]
DR Antibodypedia; 53684; 75 antibodies from 18 providers.
DR Ensembl; ENSMUST00000118515; ENSMUSP00000113141; ENSMUSG00000008140. [Q3TAS6-2]
DR Ensembl; ENSMUST00000118808; ENSMUSP00000113509; ENSMUSG00000008140. [Q3TAS6-1]
DR GeneID; 69683; -.
DR KEGG; mmu:69683; -.
DR UCSC; uc009gpq.2; mouse. [Q3TAS6-2]
DR UCSC; uc012fjp.1; mouse. [Q3TAS6-1]
DR CTD; 284361; -.
DR MGI; MGI:1916933; Emc10.
DR VEuPathDB; HostDB:ENSMUSG00000008140; -.
DR eggNOG; KOG4827; Eukaryota.
DR GeneTree; ENSGT00390000004520; -.
DR HOGENOM; CLU_065716_0_0_1; -.
DR InParanoid; Q3TAS6; -.
DR OrthoDB; 1514526at2759; -.
DR PhylomeDB; Q3TAS6; -.
DR TreeFam; TF314052; -.
DR BioGRID-ORCS; 69683; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Emc10; mouse.
DR PRO; PR:Q3TAS6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3TAS6; protein.
DR Bgee; ENSMUSG00000008140; Expressed in facial nucleus and 258 other tissues.
DR ExpressionAtlas; Q3TAS6; baseline and differential.
DR Genevisible; Q3TAS6; MM.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0032977; F:membrane insertase activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; ISS:UniProtKB.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR InterPro; IPR029615; Emc10.
DR PANTHER; PTHR21397:SF4; PTHR21397:SF4; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Angiogenesis; Endoplasmic reticulum; Membrane;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT CHAIN 26..258
FT /note="ER membrane protein complex subunit 10"
FT /id="PRO_0000315049"
FT TOPO_DOM 26..221
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT VAR_SEQ 228..258
FT /note="MYIIPVVLFLMMSGAPDAGGQGGGGGGGSSR -> HLILGGAVLLTALRPAA
FT PGPAPAPTEA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20680400"
FT /id="VSP_030475"
FT CONFLICT 73
FT /note="L -> S (in Ref. 2; BAE42592 and 3; AAH20179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 27053 MW; B110FE59563F8066 CRC64;
MVAAGAGVTR LLVLLLMVAA APSRARGSGC RVGASARGTG ADGREAEGCG TVALLLEHSF
ELGDGANFQK RGLLLWNQQD GTLSATQRQL SEEERGRLRD VAAVNGLYRV RVPRRPGTLD
GSEAGGHVSS FVPACSLVES HLSDQLTLHV DVAGNVVGLS VVVYPGGCRG SEVEDEDLEL
FNTSVQLRPP STAPGPETAA FIERLEMEQA QKAKNPQEQK SFFAKYWMYI IPVVLFLMMS
GAPDAGGQGG GGGGGSSR
