TM7S3_MOUSE
ID TM7S3_MOUSE Reviewed; 565 AA.
AC Q9CRG1; Q3TBQ2; Q3U3Q6; Q4F873; Q6PES5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Transmembrane 7 superfamily member 3;
DE AltName: Full=NARP1;
DE Flags: Precursor;
GN Name=Tm7sf3;
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].
RC STRAIN=C3H/An;
RA Chang N.-S.;
RT "Cloning and characterization of a 7-transmembrane protein NARP in the
RT nucleus.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic stem cell;
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] OF 257-565.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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.
RX PubMed=21853325; DOI=10.1007/s00125-011-2277-3;
RA Beck A., Isaac R., Lavelin I., Hart Y., Volberg T., Shatz-Azoulay H.,
RA Geiger B., Zick Y.;
RT "An siRNA screen identifies transmembrane 7 superfamily member 3 (TM7SF3),
RT a seven transmembrane orphan receptor, as an inhibitor of cytokine-induced
RT death of pancreatic beta cells.";
RL Diabetologia 54:2845-2855(2011).
RN [5]
RP FUNCTION.
RX PubMed=27740623; DOI=10.1038/cdd.2016.108;
RA Isaac R., Goldstein I., Furth N., Zilber N., Streim S., Boura-Halfon S.,
RA Elhanany E., Rotter V., Oren M., Zick Y.;
RT "TM7SF3, a novel p53-regulated homeostatic factor, attenuates cellular
RT stress and the subsequent induction of the unfolded protein response.";
RL Cell Death Differ. 24:132-143(2017).
CC -!- FUNCTION: Involved in the inhibition of cytokine-induced death of
CC pancreatic beta cells (PubMed:21853325). Involved in the promotion of
CC insulin secretion from pancreatic beta cells (By similarity). Is a
CC downstream transcriptional target of p53/TP53, and acts as a pro-
CC survival homeostatic factor that attenuates the development of cellular
CC stress. Maintains protein homeostasis and promotes cell survival
CC through attenuation of endoplasmic reticulum (ER) stress and the
CC subsequent induction of unfolded protein response (UPR)
CC (PubMed:27740623). {ECO:0000250|UniProtKB:Q9NS93,
CC ECO:0000269|PubMed:21853325, ECO:0000269|PubMed:27740623}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NS93};
CC Multi-pass membrane protein {ECO:0000255}.
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DR EMBL; DQ104329; AAZ14855.1; -; mRNA.
DR EMBL; AK010720; BAB27141.1; -; mRNA.
DR EMBL; AK154633; BAE32729.1; -; mRNA.
DR EMBL; AK171111; BAE42255.1; -; mRNA.
DR EMBL; BC057900; AAH57900.1; -; mRNA.
DR CCDS; CCDS20699.1; -.
DR RefSeq; NP_080557.2; NM_026281.2.
DR AlphaFoldDB; Q9CRG1; -.
DR SMR; Q9CRG1; -.
DR IntAct; Q9CRG1; 1.
DR MINT; Q9CRG1; -.
DR STRING; 10090.ENSMUSP00000045650; -.
DR GlyGen; Q9CRG1; 4 sites.
DR iPTMnet; Q9CRG1; -.
DR PhosphoSitePlus; Q9CRG1; -.
DR EPD; Q9CRG1; -.
DR MaxQB; Q9CRG1; -.
DR PaxDb; Q9CRG1; -.
DR PeptideAtlas; Q9CRG1; -.
DR PRIDE; Q9CRG1; -.
DR ProteomicsDB; 259232; -.
DR DNASU; 67623; -.
DR GeneID; 67623; -.
DR KEGG; mmu:67623; -.
DR UCSC; uc009ese.1; mouse.
DR CTD; 51768; -.
DR MGI; MGI:1914873; Tm7sf3.
DR eggNOG; ENOG502QS07; Eukaryota.
DR InParanoid; Q9CRG1; -.
DR OrthoDB; 1322527at2759; -.
DR PhylomeDB; Q9CRG1; -.
DR TreeFam; TF332291; -.
DR BioGRID-ORCS; 67623; 5 hits in 73 CRISPR screens.
DR PRO; PR:Q9CRG1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9CRG1; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; IMP:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:UniProtKB.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR InterPro; IPR025256; DUF4203.
DR InterPro; IPR042502; TM7SF3.
DR PANTHER; PTHR15937; PTHR15937; 1.
DR Pfam; PF13886; DUF4203; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Signal;
KW Stress response; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..565
FT /note="Transmembrane 7 superfamily member 3"
FT /id="PRO_0000022538"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 170
FT /note="T -> A (in Ref. 1; AAZ14855 and 2; BAE42255)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="S -> F (in Ref. 2; BAB27141/BAE32729)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="F -> V (in Ref. 2; BAB27141/BAE32729)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="V -> I (in Ref. 2; BAB27141/BAE32729)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="Q -> K (in Ref. 2; BAE42255)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="F -> V (in Ref. 2; BAB27141/BAE32729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 63251 MW; EBAD9EF756DF9C76 CRC64;
MWRLRLLVLA VLAAGSAEAQ ANSSDGFLEF SVGKFTYFVL SKSSPQEAVL RHISSNVTFL
LFQIHSQYQN TTVSFTKTLL PSTSGTGNDR GLVFILRPEQ AVCTWYLETG DTKPVQSVAL
TLSYSERDPI PGGCNLEFDL DIDPNLYLDY NFFETTIKFA PANIGYARAT EPPPCDVSTS
RESRWRLRYD VYQYFLPEGD LTEASLLHHL QRMAQVAQVK ASAIKVATLT ADDKTAVSFS
SLPGQGVIYN VIVWDPSLNT SAAYVPVHTY ACSFESVDGN CASPGRVSTK VFSTLFALLG
LFVCFFGHRF WKTDLFFVGF IFLGFFFYIL ITRLTPLQYD VRLALTAVAG SFGGLLLVAS
WWRFGILTLC MLCVGLVLGF LVSSGTFFTP LGNLNVFHDD GVFWVTFSCI ALLVPVIFMG
CLRILNILAC GVVGSYSVVL AVNSYMFTSL SYITLNVLRR ALNTDFRGAF IRVPFQTNDY
IILAVWGMLA VSGITLQIRR ERGQPPFPPH PYKLWKQERE RRVTNILDPS HHIPPLRERL
YGRVARIKEL FQKEQPAGER TPLLL
