TM9S2_RAT
ID TM9S2_RAT Reviewed; 663 AA.
AC Q66HG5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Transmembrane 9 superfamily member 2;
DE Flags: Precursor;
GN Name=Tm9sf2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP SUBCELLULAR LOCATION.
RX PubMed=31522887; DOI=10.1016/j.cell.2019.08.025;
RA Fu M.M., McAlear T.S., Nguyen H., Oses-Prieto J.A., Valenzuela A.,
RA Shi R.D., Perrino J.J., Huang T.T., Burlingame A.L., Bechstedt S.,
RA Barres B.A.;
RT "The Golgi outpost protein TPPP nucleates microtubules and is critical for
RT myelination.";
RL Cell 0:0-0(2019).
CC -!- FUNCTION: In the intracellular compartments, may function as a channel
CC or small molecule transporter. {ECO:0000250|UniProtKB:Q99805}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q99805};
CC Multi-pass membrane protein {ECO:0000255}. Golgi outpost
CC {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000269|PubMed:31522887}. 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:0000269|PubMed:31522887}.
CC -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC {ECO:0000305}.
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DR EMBL; BC081873; AAH81873.1; -; mRNA.
DR RefSeq; NP_001005554.1; NM_001005554.1.
DR AlphaFoldDB; Q66HG5; -.
DR IntAct; Q66HG5; 1.
DR STRING; 10116.ENSRNOP00000017211; -.
DR SwissPalm; Q66HG5; -.
DR jPOST; Q66HG5; -.
DR PaxDb; Q66HG5; -.
DR PRIDE; Q66HG5; -.
DR Ensembl; ENSRNOT00000017211; ENSRNOP00000017211; ENSRNOG00000012751.
DR GeneID; 306197; -.
DR KEGG; rno:306197; -.
DR CTD; 9375; -.
DR RGD; 1359230; Tm9sf2.
DR eggNOG; KOG1278; Eukaryota.
DR GeneTree; ENSGT00940000157563; -.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; Q66HG5; -.
DR OMA; TILITYH; -.
DR OrthoDB; 641127at2759; -.
DR PRO; PR:Q66HG5; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000012751; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q66HG5; RN.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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:0006672; P:ceramide metabolic process; ISO:RGD.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISO:RGD.
DR GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR GO; GO:0010908; P:regulation of heparan sulfate proteoglycan biosynthetic process; ISO:RGD.
DR InterPro; IPR004240; EMP70.
DR PANTHER; PTHR10766; PTHR10766; 1.
DR Pfam; PF02990; EMP70; 1.
PE 2: Evidence at transcript 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_0000034368"
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; 75586 MW; D10FD1885D85AFD1 CRC64;
MSSRPPASLP ARGPRLLLLS LLLLGTVPGP RPGSAFYLPG LAPVNFCTEE KKSNECKAEI
ELFVNRLDSV ESVLPYEYTA FDFCQASEGK RPSENLGQVL FGERIEPSPY KFTFNKEETC
KLVCTKTYHT EKAEDKQKLD FLKKSMLLNY QHHWIVDNMP VTWCYEVEDN QKFCNPGFPI
GCYITDKGHA KDACVISSEF HERDTFYIFN HVDIKIQYHV VETGSMGARL VAAKLEPKSF
RHTHIDKPDC SGPAMDISNK ASGEIKIAYT YSISFEEEKN 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
VYFLVYAIHY FFSKLQITGT ASTILYFGYT MIMVLIFFLF TGTIGFFACF WFVTKIYSVV
KVD
