TM39A_HUMAN
ID TM39A_HUMAN Reviewed; 488 AA.
AC Q9NV64; D3DN80; Q53FN4; Q53GI1; Q6PKB5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transmembrane protein 39A;
GN Name=TMEM39A; Synonyms=SUSR2 {ECO:0000303|PubMed:31806350};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-487.
RC TISSUE=Gastric mucosa, and Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
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 [5]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-247.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=28133515; DOI=10.5487/tr.2017.33.1.063;
RA Park J., Lee H., Tran Q., Mun K., Kim D., Hong Y., Kwon S.H., Brazil D.,
RA Park J., Kim S.H.;
RT "Recognition of Transmembrane Protein 39A as a Tumor-Specific Marker in
RT Brain Tumor.";
RL Toxicol. Res. 33:63-69(2017).
RN [7]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EMCV CAPSID PROTEINS
RP VP1 AND VP2 (MICROBIAL INFECTION).
RX PubMed=31849860; DOI=10.3389/fmicb.2019.02680;
RA Li X., Ma R., Li Q., Li S., Zhang H., Xie J., Bai J., Idris A., Feng R.;
RT "Transmembrane Protein 39A Promotes the Replication of Encephalomyocarditis
RT Virus via Autophagy Pathway.";
RL Front. Microbiol. 10:2680-2680(2019).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SACM1L; SEC23A AND
RP SEC24A.
RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA Miao G., Zhang Y., Chen D., Zhang H.;
RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Regulates autophagy by controlling the spatial distribution
CC and levels of the intracellular phosphatidylinositol 4-phosphate
CC (PtdIns(4)P) pools (PubMed:31806350). Modulates (PtdIns(4)P) levels by
CC regulating the ER-to-Golgi trafficking of the phosphatidylinositide
CC phosphatase SACM1L (PubMed:31806350). {ECO:0000269|PubMed:31806350}.
CC -!- FUNCTION: (Microbial infection) Positively regulates the replication of
CC encephalomyocarditis virus (EMCV) via autophagy-dependent pathway.
CC {ECO:0000269|PubMed:31849860}.
CC -!- SUBUNIT: Interacts with SACM1L, SEC23A and SEC24A.
CC {ECO:0000269|PubMed:31806350}.
CC -!- SUBUNIT: (Microbial infection) Interacts with encephalomyocarditis
CC virus (EMCV) major capsid proteins VP1 and VP2.
CC {ECO:0000269|PubMed:31849860}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:31806350}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NV64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NV64-2; Sequence=VSP_023416, VSP_023417;
CC -!- TISSUE SPECIFICITY: Up-regulated in brain tumor glioblastoma multiforme
CC cells (at protein level). {ECO:0000269|PubMed:28133515}.
CC -!- SIMILARITY: Belongs to the TMEM39 family. {ECO:0000305}.
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DR EMBL; AK001764; BAA91893.1; -; mRNA.
DR EMBL; AK223248; BAD96968.1; -; mRNA.
DR EMBL; AK222950; BAD96670.1; -; mRNA.
DR EMBL; CH471052; EAW79571.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79572.1; -; Genomic_DNA.
DR EMBL; BC003192; AAH03192.1; -; mRNA.
DR EMBL; BC021277; AAH21277.1; -; mRNA.
DR CCDS; CCDS2987.1; -. [Q9NV64-1]
DR RefSeq; NP_060736.1; NM_018266.2. [Q9NV64-1]
DR RefSeq; XP_006713750.1; XM_006713687.1. [Q9NV64-1]
DR AlphaFoldDB; Q9NV64; -.
DR BioGRID; 120545; 54.
DR IntAct; Q9NV64; 24.
DR STRING; 9606.ENSP00000326063; -.
DR TCDB; 9.B.385.1.1; the tmem39a or susr2 (tmem39a) family.
DR GlyGen; Q9NV64; 2 sites.
DR iPTMnet; Q9NV64; -.
DR PhosphoSitePlus; Q9NV64; -.
DR BioMuta; TMEM39A; -.
DR DMDM; 74734456; -.
DR EPD; Q9NV64; -.
DR jPOST; Q9NV64; -.
DR MassIVE; Q9NV64; -.
DR MaxQB; Q9NV64; -.
DR PaxDb; Q9NV64; -.
DR PeptideAtlas; Q9NV64; -.
DR PRIDE; Q9NV64; -.
DR ProteomicsDB; 82750; -. [Q9NV64-1]
DR ProteomicsDB; 82751; -. [Q9NV64-2]
DR Antibodypedia; 49908; 25 antibodies from 12 providers.
DR DNASU; 55254; -.
DR Ensembl; ENST00000319172.10; ENSP00000326063.5; ENSG00000176142.13. [Q9NV64-1]
DR Ensembl; ENST00000438581.6; ENSP00000402149.2; ENSG00000176142.13. [Q9NV64-2]
DR GeneID; 55254; -.
DR KEGG; hsa:55254; -.
DR MANE-Select; ENST00000319172.10; ENSP00000326063.5; NM_018266.3; NP_060736.1.
DR UCSC; uc003eck.3; human. [Q9NV64-1]
DR CTD; 55254; -.
DR DisGeNET; 55254; -.
DR GeneCards; TMEM39A; -.
DR HGNC; HGNC:25600; TMEM39A.
DR HPA; ENSG00000176142; Low tissue specificity.
DR neXtProt; NX_Q9NV64; -.
DR OpenTargets; ENSG00000176142; -.
DR PharmGKB; PA134956032; -.
DR VEuPathDB; HostDB:ENSG00000176142; -.
DR eggNOG; KOG3828; Eukaryota.
DR GeneTree; ENSGT00390000018895; -.
DR HOGENOM; CLU_028992_0_0_1; -.
DR InParanoid; Q9NV64; -.
DR OMA; PQHLWSE; -.
DR OrthoDB; 1460710at2759; -.
DR PhylomeDB; Q9NV64; -.
DR TreeFam; TF321110; -.
DR PathwayCommons; Q9NV64; -.
DR SignaLink; Q9NV64; -.
DR BioGRID-ORCS; 55254; 15 hits in 1080 CRISPR screens.
DR ChiTaRS; TMEM39A; human.
DR GenomeRNAi; 55254; -.
DR Pharos; Q9NV64; Tbio.
DR PRO; PR:Q9NV64; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NV64; protein.
DR Bgee; ENSG00000176142; Expressed in stromal cell of endometrium and 171 other tissues.
DR ExpressionAtlas; Q9NV64; baseline and differential.
DR Genevisible; Q9NV64; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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; IMP:UniProtKB.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IDA:UniProtKB.
DR InterPro; IPR019397; Uncharacterised_TMEM39.
DR PANTHER; PTHR12995; PTHR12995; 1.
DR Pfam; PF10271; Tmp39; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..488
FT /note="Transmembrane protein 39A"
FT /id="PRO_0000279224"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 141..146
FT /note="ATKAGA -> VCVCKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023416"
FT VAR_SEQ 147..488
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023417"
FT VARIANT 247
FT /note="S -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036095"
FT VARIANT 487
FT /note="A -> T (in dbSNP:rs1132200)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_030871"
FT CONFLICT 79
FT /note="F -> L (in Ref. 2; BAD96968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55667 MW; EC3EB5D8B05ED09B CRC64;
MPGGRRGPSR QQLSRSALPS LQTLVGGGCG NGTGLRNRNG SAIGLPVPPI TALITPGPVR
HCQIPDLPVD GSLLFEFLFF IYLLVALFIQ YINIYKTVWW YPYNHPASCT SLNFHLIDYH
LAAFITVMLA RRLVWALISE ATKAGAASMI HYMVLISARL VLLTLCGWVL CWTLVNLFRS
HSVLNLLFLG YPFGVYVPLC CFHQDSRAHL LLTDYNYVVQ HEAVEESAST VGGLAKSKDF
LSLLLESLKE QFNNATPIPT HSCPLSPDLI RNEVECLKAD FNHRIKEVLF NSLFSAYYVA
FLPLCFVKST QYYDMRWSCE HLIMVWINAF VMLTTQLLPS KYCDLLHKSA AHLGKWQKLE
HGSYSNAPQH IWSENTIWPQ GVLVRHSRCL YRAMGPYNVA VPSDVSHARF YFLFHRPLRL
LNLLILIEGS VVFYQLYSLL RSEKWNHTLS MALILFCNYY VLFKLLRDRI VLGRAYSYPL
NSYELKAN
