TM245_RAT
ID TM245_RAT Reviewed; 876 AA.
AC D3ZXD8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Transmembrane protein 245;
GN Name=Tmem245;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86)
CC family. {ECO:0000305}.
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DR EMBL; AABR03042316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03042476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03046793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03041614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003749993.1; XM_003749945.3.
DR RefSeq; XP_003754079.1; XM_003754031.3.
DR AlphaFoldDB; D3ZXD8; -.
DR STRING; 10116.ENSRNOP00000063739; -.
DR GlyGen; D3ZXD8; 3 sites.
DR iPTMnet; D3ZXD8; -.
DR PhosphoSitePlus; D3ZXD8; -.
DR PaxDb; D3ZXD8; -.
DR PRIDE; D3ZXD8; -.
DR Ensembl; ENSRNOT00000032299; ENSRNOP00000035996; ENSRNOG00000026271.
DR GeneID; 298020; -.
DR KEGG; rno:298020; -.
DR UCSC; RGD:1308958; rat.
DR CTD; 23731; -.
DR RGD; 1308958; Tmem245.
DR eggNOG; KOG2365; Eukaryota.
DR GeneTree; ENSGT00390000001667; -.
DR HOGENOM; CLU_005960_0_0_1; -.
DR InParanoid; D3ZXD8; -.
DR OrthoDB; 228524at2759; -.
DR PhylomeDB; D3ZXD8; -.
DR PRO; PR:D3ZXD8; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000026271; Expressed in heart and 18 other tissues.
DR ExpressionAtlas; D3ZXD8; baseline and differential.
DR Genevisible; D3ZXD8; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR002549; AI-2E-like.
DR PANTHER; PTHR21716; PTHR21716; 1.
DR Pfam; PF01594; AI-2E_transport; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT CHAIN 2..876
FT /note="Transmembrane protein 245"
FT /id="PRO_0000417170"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 876 AA; 97282 MW; 9C8B17D76E93961E CRC64;
MADRGGPAEE PSPRGSPRSE PRVPRTAGPS ETPRTAALAL RFDKPIKQAF YNTGAVLFVC
LCCGAAVLVY FILEAFLRPL LWAVLCGTFL HPFKSSLTRL GRLWLRRLHR AHTPIVLAAL
LLPLCFADYG VEALGEQALR RRRLLLLLGA GGPLLYGLYC LGSYLGVQVL LAHAGALICR
GLDYFSSLWI WTLVVGYVLM VSFKWNASTQ HYLRAVSIPV WMILLFHIAS LAGSWRIPVF
LVIVFLMSAG TLYEKQNEKE SAGAELPGQV ISMAASTLAN LAISITGYES SSEDQPSDPS
AEPTDKGEPP PAPSASSSSS SRSSPSSPSP TLGRQRPEMG TFLRKKKTSD IYFVSLVWAI
IAVQLWLNLW IVQLLPVPVA VWIIKKLVIH FGVVGFLEKR CRAWWQVMES FLKERQEALA
PWPITGLGKF LLKVDSKLWH WLNKKMIIWL EKMLDKIISI FIIFLLVIGT LLLALLLTAK
VHQESVHMIE VTSSLINETL ANHPEWANWL PEAQVVQRAL NSAANNVYQY GREWITHKLH
KILGDKVNNT AVIEKQVLEL WDRLYHSWFV KNVTHSGRHK GHKMHVSRQN SWLGDILDWQ
DIASFVHENI ETFLSILESL WIVMSRNVSL LFTTVTTLLT ILFYSGTALL NFVLSLIIFL
TTLFYLLSSS DEYYKPVKWV ISLTPLSQPG PSSNIIGQSV EEAIRGVFDA SLKMAGFYGL
YTWLTHTVFG INIVFIPSAL AAILGAVPFL GTYWAAVPAV LDLWLTQGLG CKAVLLLVFH
LLPTYFVDTA IYSDISGGGH PYLTGLAVAG GAYYLGLEGA IIGPILLCIL VVASNIYSAM
LVSPTNSMPT PSQTPWPAQT QRTFRDISED LKSSVD
