TM9S2_HUMAN
ID TM9S2_HUMAN Reviewed; 663 AA.
AC Q99805; A8K399; Q2TAY5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transmembrane 9 superfamily member 2;
DE AltName: Full=p76;
DE Flags: Precursor;
GN Name=TM9SF2;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9729438; DOI=10.1016/s0378-1119(98)00349-7;
RA Schimmoeller F., Diaz E., Muehlbauer B., Pfeffer S.R.;
RT "Characterization of a 76 kDa endosomal, multispanning membrane protein
RT that is highly conserved throughout evolution.";
RL Gene 216:311-318(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: In the intracellular compartments, may function as a channel
CC or small molecule transporter. {ECO:0000305|PubMed:9729438}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305|PubMed:9729438};
CC Multi-pass membrane protein {ECO:0000255}. Golgi outpost
CC {ECO:0000250|UniProtKB:Q66HG5}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:Q66HG5}. Note=Localizes to the
CC postsynaptic Golgi apparatus region, also named Golgi outpost, which
CC shapes dendrite morphology by functioning as sites of acentrosomal
CC microtubule nucleation. {ECO:0000250|UniProtKB:Q66HG5}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Especially abundant in
CC pancreas, highly expressed in kidney, lower levels in heart, brain,
CC skeletal muscle and placenta. Lowest expression in lung and liver.
CC {ECO:0000269|PubMed:9729438}.
CC -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC {ECO:0000305}.
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DR EMBL; U81006; AAB38973.1; -; mRNA.
DR EMBL; AK290514; BAF83203.1; -; mRNA.
DR EMBL; AL139035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110656; AAI10657.1; -; mRNA.
DR EMBL; BC130293; AAI30294.1; -; mRNA.
DR CCDS; CCDS9493.1; -.
DR RefSeq; NP_004791.1; NM_004800.2.
DR AlphaFoldDB; Q99805; -.
DR BioGRID; 114776; 82.
DR IntAct; Q99805; 27.
DR MINT; Q99805; -.
DR STRING; 9606.ENSP00000365567; -.
DR TCDB; 8.A.68.1.6; the endomembrane protein-70 (emp70) family.
DR iPTMnet; Q99805; -.
DR PhosphoSitePlus; Q99805; -.
DR SwissPalm; Q99805; -.
DR BioMuta; TM9SF2; -.
DR DMDM; 13878805; -.
DR EPD; Q99805; -.
DR jPOST; Q99805; -.
DR MassIVE; Q99805; -.
DR MaxQB; Q99805; -.
DR PaxDb; Q99805; -.
DR PeptideAtlas; Q99805; -.
DR PRIDE; Q99805; -.
DR ProteomicsDB; 78484; -.
DR Antibodypedia; 970; 75 antibodies from 17 providers.
DR DNASU; 9375; -.
DR Ensembl; ENST00000376387.5; ENSP00000365567.3; ENSG00000125304.10.
DR Ensembl; ENST00000642475.1; ENSP00000493515.1; ENSG00000125304.10.
DR GeneID; 9375; -.
DR KEGG; hsa:9375; -.
DR MANE-Select; ENST00000376387.5; ENSP00000365567.3; NM_004800.3; NP_004791.1.
DR UCSC; uc001voj.3; human.
DR CTD; 9375; -.
DR DisGeNET; 9375; -.
DR GeneCards; TM9SF2; -.
DR HGNC; HGNC:11865; TM9SF2.
DR HPA; ENSG00000125304; Low tissue specificity.
DR MIM; 604678; gene.
DR neXtProt; NX_Q99805; -.
DR OpenTargets; ENSG00000125304; -.
DR PharmGKB; PA36566; -.
DR VEuPathDB; HostDB:ENSG00000125304; -.
DR eggNOG; KOG1278; Eukaryota.
DR GeneTree; ENSGT00940000157563; -.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; Q99805; -.
DR OMA; TILITYH; -.
DR OrthoDB; 641127at2759; -.
DR PhylomeDB; Q99805; -.
DR TreeFam; TF300394; -.
DR PathwayCommons; Q99805; -.
DR SignaLink; Q99805; -.
DR BioGRID-ORCS; 9375; 73 hits in 1081 CRISPR screens.
DR ChiTaRS; TM9SF2; human.
DR GeneWiki; TM9SF2; -.
DR GenomeRNAi; 9375; -.
DR Pharos; Q99805; Tbio.
DR PRO; PR:Q99805; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q99805; protein.
DR Bgee; ENSG00000125304; Expressed in mucosa of sigmoid colon and 213 other tissues.
DR ExpressionAtlas; Q99805; baseline and differential.
DR Genevisible; Q99805; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; TAS:ProtInc.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006672; P:ceramide metabolic process; IMP:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR GO; GO:0010908; P:regulation of heparan sulfate proteoglycan biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR004240; EMP70.
DR PANTHER; PTHR10766; PTHR10766; 1.
DR Pfam; PF02990; EMP70; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..663
FT /note="Transmembrane 9 superfamily member 2"
FT /id="PRO_0000034365"
FT TOPO_DOM 29..300
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..466
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..554
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 576..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..631
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 663 AA; 75776 MW; C21A4D224534734D CRC64;
MSARLPVLSP PRWPRLLLLS LLLLGAVPGP RRSGAFYLPG LAPVNFCDEE KKSDECKAEI
ELFVNRLDSV ESVLPYEYTA FDFCQASEGK RPSENLGQVL FGERIEPSPY KFTFNKKETC
KLVCTKTYHT EKAEDKQKLE FLKKSMLLNY QHHWIVDNMP VTWCYDVEDG QRFCNPGFPI
GCYITDKGHA KDACVISSDF HERDTFYIFN HVDIKIYYHV VETGSMGARL VAAKLEPKSF
KHTHIDKPDC SGPPMDISNK ASGEIKIAYT YSVSFEEDDK IRWASRWDYI LESMPHTHIQ
WFSIMNSLVI VLFLSGMVAM IMLRTLHKDI ARYNQMDSTE DAQEEFGWKL VHGDIFRPPR
KGMLLSVFLG SGTQILIMTF VTLFFACLGF LSPANRGALM TCAVVLWVLL GTPAGYVAAR
FYKSFGGEKW KTNVLLTSFL CPGIVFADFF IMNLILWGEG SSAAIPFGTL VAILALWFCI
SVPLTFIGAY FGFKKNAIEH PVRTNQIPRQ IPEQSFYTKP LPGIIMGGIL PFGCIFIQLF
FILNSIWSHQ MYYMFGFLFL VFIILVITCS EATILLCYFH LCAEDYHWQW RSFLTSGFTA
VYFLIYAVHY FFSKLQITGT ASTILYFGYT MIMVLIFFLF TGTIGFFACF WFVTKIYSVV
KVD
