TM39A_MOUSE
ID TM39A_MOUSE Reviewed; 486 AA.
AC Q9CYC3; Q3TFJ2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transmembrane protein 39A;
GN Name=Tmem39a;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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).
CC -!- FUNCTION: Regulates autophagy by controlling the spatial distribution
CC and levels of the intracellular phosphatidylinositol 4-phosphate
CC (PtdIns(4)P) pools (By similarity). Modulates (PtdIns(4)P) levels by
CC regulating the ER-to-Golgi trafficking of the phosphatidylinositide
CC phosphatase SACM1L (By similarity). {ECO:0000250|UniProtKB:Q9NV64}.
CC -!- SUBUNIT: Interacts with SACM1L, SEC23A and SEC24A.
CC {ECO:0000250|UniProtKB:Q9NV64}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NV64}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CYC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CYC3-2; Sequence=VSP_023418;
CC -!- SIMILARITY: Belongs to the TMEM39 family. {ECO:0000305}.
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DR EMBL; AK017817; BAB30953.1; -; mRNA.
DR EMBL; AK160576; BAE35884.1; -; mRNA.
DR EMBL; AK169127; BAE40906.1; -; mRNA.
DR EMBL; BC020318; AAH20318.1; -; mRNA.
DR CCDS; CCDS28171.1; -. [Q9CYC3-1]
DR CCDS; CCDS57029.1; -. [Q9CYC3-2]
DR RefSeq; NP_001192215.1; NM_001205286.1. [Q9CYC3-1]
DR RefSeq; NP_001192216.1; NM_001205287.1. [Q9CYC3-2]
DR RefSeq; NP_080683.2; NM_026407.3. [Q9CYC3-1]
DR AlphaFoldDB; Q9CYC3; -.
DR STRING; 10090.ENSMUSP00000002924; -.
DR GlyGen; Q9CYC3; 1 site.
DR iPTMnet; Q9CYC3; -.
DR PhosphoSitePlus; Q9CYC3; -.
DR EPD; Q9CYC3; -.
DR MaxQB; Q9CYC3; -.
DR PaxDb; Q9CYC3; -.
DR PRIDE; Q9CYC3; -.
DR ProteomicsDB; 259228; -. [Q9CYC3-1]
DR ProteomicsDB; 259229; -. [Q9CYC3-2]
DR Antibodypedia; 49908; 25 antibodies from 12 providers.
DR DNASU; 67846; -.
DR Ensembl; ENSMUST00000002924; ENSMUSP00000002924; ENSMUSG00000002845. [Q9CYC3-1]
DR Ensembl; ENSMUST00000163884; ENSMUSP00000132515; ENSMUSG00000002845. [Q9CYC3-1]
DR Ensembl; ENSMUST00000171687; ENSMUSP00000126218; ENSMUSG00000002845. [Q9CYC3-2]
DR GeneID; 67846; -.
DR KEGG; mmu:67846; -.
DR UCSC; uc007zfe.2; mouse. [Q9CYC3-1]
DR UCSC; uc007zff.2; mouse. [Q9CYC3-2]
DR CTD; 55254; -.
DR MGI; MGI:1915096; Tmem39a.
DR VEuPathDB; HostDB:ENSMUSG00000002845; -.
DR eggNOG; KOG3828; Eukaryota.
DR GeneTree; ENSGT00390000018895; -.
DR HOGENOM; CLU_028992_0_0_1; -.
DR InParanoid; Q9CYC3; -.
DR OMA; PQHLWSE; -.
DR OrthoDB; 1460710at2759; -.
DR PhylomeDB; Q9CYC3; -.
DR TreeFam; TF321110; -.
DR BioGRID-ORCS; 67846; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9CYC3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CYC3; protein.
DR Bgee; ENSMUSG00000002845; Expressed in humerus cartilage element and 216 other tissues.
DR ExpressionAtlas; Q9CYC3; baseline and differential.
DR Genevisible; Q9CYC3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR InterPro; IPR019397; Uncharacterised_TMEM39.
DR PANTHER; PTHR12995; PTHR12995; 1.
DR Pfam; PF10271; Tmp39; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autophagy; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..486
FT /note="Transmembrane protein 39A"
FT /id="PRO_0000279225"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 193..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023418"
FT CONFLICT 81
FT /note="I -> T (in Ref. 1; BAE40906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 55720 MW; 064DD79EBF294FC3 CRC64;
MPSRRRGPSR QQLSRSALPS IQTLVGGGCG NGTGLRNRNG NAIGLPVPPT TALITPGPVR
HCQIPDLPVD GSLFFEFLFF IYLLIVLFIQ YINIYKTVWW YPYNHPASCT SLNFHLIDYY
LAAFITVMLA RRLVWALISE ATKAGAASTV HYTALILARL VLLTLCGWVL CWTLVNLFRS
HSVLNLLFLG YPFGVYVPLY CFHQDSRAHL LLTDYVVQHQ AVEEAASNVG SLARSKDFLS
LLLESLKEQF NNATPIPTHS CPLSPDLIRN EVECLKADFN HRIKEVLFNS LFSAYYVAFL
PLCFVKSTQY YDMRWSCEHL IMVWINAFVM LTTQLLPSKY CDLLHKSAAH LGKWQKLEHG
FYSNAPQHIW SENTIWPQGV LVRHSRCLYR AMGPYNVAVP SDVSHARFYF LFHRPLRVLN
LLILIEGSVV FYQLYSLLRS EKWNHTLSMA LILFCNYYVL FKLLRDRIVL GRAYSYPLNS
YELKAN
