Full text data of SERINC1
SERINC1
(KIAA1253, TDE1L, TDE2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Serine incorporator 1 (Tumor differentially expressed protein 1-like; Tumor differentially expressed protein 2)
Serine incorporator 1 (Tumor differentially expressed protein 1-like; Tumor differentially expressed protein 2)
UniProt
Q9NRX5
ID SERC1_HUMAN Reviewed; 453 AA.
AC Q9NRX5; B3KY69; E1P565; O75655; Q7Z2F5; Q8TAG1; Q9NTH8; Q9ULG7;
read moreDT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Serine incorporator 1;
DE AltName: Full=Tumor differentially expressed protein 1-like;
DE AltName: Full=Tumor differentially expressed protein 2;
GN Name=SERINC1; Synonyms=KIAA1253, TDE1L, TDE2; ORFNames=UNQ396/PRO732;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang M., Yu L., Wu Q., Zheng L.H., Wei Y.H., Wan B., Zhao S.Y.;
RT "Identification and characterization of TDE2, a plasma-membrane
RT protein with 11 transmembrane helices, and its variable expression in
RT human lung cancer and liver cancer tissues.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; THR-352; SER-361
RP AND SER-364, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-298, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
CC -!- FUNCTION: Enhances the incorporation of serine into
CC phosphatidylserine and sphingolipids (By similarity).
CC -!- SUBUNIT: Interacts with SPTLC1 (By similarity).
CC -!- INTERACTION:
CC Q06710:PAX8; NbExp=2; IntAct=EBI-2683145, EBI-2683132;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the TDE1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86567.1; Type=Erroneous initiation;
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DR EMBL; AF087902; AAP97200.1; -; mRNA.
DR EMBL; AF092436; AAP97211.1; -; Genomic_DNA.
DR EMBL; AB033079; BAA86567.1; ALT_INIT; mRNA.
DR EMBL; AL137261; CAB70662.2; -; mRNA.
DR EMBL; AF164794; AAF80758.1; -; mRNA.
DR EMBL; AY358429; AAQ88795.1; -; mRNA.
DR EMBL; AK128781; BAG54731.1; -; mRNA.
DR EMBL; Z99129; CAD92585.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48172.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48173.1; -; Genomic_DNA.
DR EMBL; BC028607; AAH28607.1; -; mRNA.
DR EMBL; BC033029; AAH33029.1; -; mRNA.
DR RefSeq; NP_065806.1; NM_020755.2.
DR UniGene; Hs.146668; -.
DR ProteinModelPortal; Q9NRX5; -.
DR IntAct; Q9NRX5; 9.
DR MINT; MINT-5005668; -.
DR STRING; 9606.ENSP00000342962; -.
DR PhosphoSite; Q9NRX5; -.
DR DMDM; 25453298; -.
DR PaxDb; Q9NRX5; -.
DR PRIDE; Q9NRX5; -.
DR DNASU; 57515; -.
DR Ensembl; ENST00000339697; ENSP00000342962; ENSG00000111897.
DR Ensembl; ENST00000368454; ENSP00000357439; ENSG00000111897.
DR GeneID; 57515; -.
DR KEGG; hsa:57515; -.
DR UCSC; uc003pyy.1; human.
DR CTD; 57515; -.
DR GeneCards; GC06M122807; -.
DR HGNC; HGNC:13464; SERINC1.
DR HPA; HPA035738; -.
DR HPA; HPA035739; -.
DR MIM; 614548; gene.
DR neXtProt; NX_Q9NRX5; -.
DR PharmGKB; PA134973249; -.
DR eggNOG; NOG308011; -.
DR HOVERGEN; HBG025699; -.
DR InParanoid; Q9NRX5; -.
DR OMA; SKWPSVW; -.
DR OrthoDB; EOG7TXKGQ; -.
DR PhylomeDB; Q9NRX5; -.
DR ChiTaRS; SERINC1; human.
DR GeneWiki; SERINC1; -.
DR GenomeRNAi; 57515; -.
DR NextBio; 63885; -.
DR PRO; PR:Q9NRX5; -.
DR Bgee; Q9NRX5; -.
DR CleanEx; HS_SERINC1; -.
DR Genevestigator; Q9NRX5; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; ISS:HGNC.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:HGNC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051347; P:positive regulation of transferase activity; ISS:HGNC.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:HGNC.
DR InterPro; IPR005016; TMS_TDE.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR Pfam; PF03348; Serinc; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane;
KW Myristate; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 453 Serine incorporator 1.
FT /FTId=PRO_0000218966.
FT TOPO_DOM 2 39 Cytoplasmic (Potential).
FT TRANSMEM 40 60 Helical; (Potential).
FT TOPO_DOM 61 88 Lumenal (Potential).
FT TRANSMEM 89 109 Helical; (Potential).
FT TOPO_DOM 110 123 Cytoplasmic (Potential).
FT TRANSMEM 124 144 Helical; (Potential).
FT TOPO_DOM 145 151 Lumenal (Potential).
FT TRANSMEM 152 172 Helical; (Potential).
FT TOPO_DOM 173 197 Cytoplasmic (Potential).
FT TRANSMEM 198 218 Helical; (Potential).
FT TOPO_DOM 219 231 Lumenal (Potential).
FT TRANSMEM 232 252 Helical; (Potential).
FT TOPO_DOM 253 259 Cytoplasmic (Potential).
FT TRANSMEM 260 280 Helical; (Potential).
FT TOPO_DOM 281 309 Lumenal (Potential).
FT TRANSMEM 310 330 Helical; (Potential).
FT TOPO_DOM 331 387 Cytoplasmic (Potential).
FT TRANSMEM 388 408 Helical; (Potential).
FT TOPO_DOM 409 426 Lumenal (Potential).
FT TRANSMEM 427 447 Helical; (Potential).
FT TOPO_DOM 448 453 Cytoplasmic (Potential).
FT MOD_RES 351 351 Phosphoserine.
FT MOD_RES 352 352 Phosphothreonine.
FT MOD_RES 361 361 Phosphoserine.
FT MOD_RES 364 364 Phosphoserine.
FT LIPID 2 2 N-myristoyl glycine.
FT CARBOHYD 298 298 N-linked (GlcNAc...).
FT VARIANT 199 199 L -> V (in dbSNP:rs13210569).
FT /FTId=VAR_052275.
FT VARIANT 216 216 F -> V (in dbSNP:rs13210446).
FT /FTId=VAR_052276.
FT VARIANT 225 225 S -> G (in dbSNP:rs17260829).
FT /FTId=VAR_052277.
FT CONFLICT 89 89 A -> S (in Ref. 9; AAH28607).
FT CONFLICT 247 247 S -> F (in Ref. 1; AAP97200/AAP97211).
FT CONFLICT 408 408 Y -> S (in Ref. 5; AAQ88795).
SQ SEQUENCE 453 AA; 50495 MW; 3868DBF38165B78C CRC64;
MGSVLGLCSM ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG
MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA
VHNGFWFFKF AAAIAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE
SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAIVLFFVYY THPASCSENK AFISVNMLLC
VGASVMSILP KIQESQPRSG LLQSSVITVY TMYLTWSAMT NEPETNCNPS LLSIIGYNTT
STVPKEGQSV QWWHAQGIIG LILFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGGAR
SDGSLEDGDD VHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
TAVWVKISSS WIGIVLYVWT LVAPLVLTNR DFD
//
ID SERC1_HUMAN Reviewed; 453 AA.
AC Q9NRX5; B3KY69; E1P565; O75655; Q7Z2F5; Q8TAG1; Q9NTH8; Q9ULG7;
read moreDT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Serine incorporator 1;
DE AltName: Full=Tumor differentially expressed protein 1-like;
DE AltName: Full=Tumor differentially expressed protein 2;
GN Name=SERINC1; Synonyms=KIAA1253, TDE1L, TDE2; ORFNames=UNQ396/PRO732;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang M., Yu L., Wu Q., Zheng L.H., Wei Y.H., Wan B., Zhao S.Y.;
RT "Identification and characterization of TDE2, a plasma-membrane
RT protein with 11 transmembrane helices, and its variable expression in
RT human lung cancer and liver cancer tissues.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; THR-352; SER-361
RP AND SER-364, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-298, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
CC -!- FUNCTION: Enhances the incorporation of serine into
CC phosphatidylserine and sphingolipids (By similarity).
CC -!- SUBUNIT: Interacts with SPTLC1 (By similarity).
CC -!- INTERACTION:
CC Q06710:PAX8; NbExp=2; IntAct=EBI-2683145, EBI-2683132;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the TDE1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86567.1; Type=Erroneous initiation;
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DR EMBL; AF087902; AAP97200.1; -; mRNA.
DR EMBL; AF092436; AAP97211.1; -; Genomic_DNA.
DR EMBL; AB033079; BAA86567.1; ALT_INIT; mRNA.
DR EMBL; AL137261; CAB70662.2; -; mRNA.
DR EMBL; AF164794; AAF80758.1; -; mRNA.
DR EMBL; AY358429; AAQ88795.1; -; mRNA.
DR EMBL; AK128781; BAG54731.1; -; mRNA.
DR EMBL; Z99129; CAD92585.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48172.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48173.1; -; Genomic_DNA.
DR EMBL; BC028607; AAH28607.1; -; mRNA.
DR EMBL; BC033029; AAH33029.1; -; mRNA.
DR RefSeq; NP_065806.1; NM_020755.2.
DR UniGene; Hs.146668; -.
DR ProteinModelPortal; Q9NRX5; -.
DR IntAct; Q9NRX5; 9.
DR MINT; MINT-5005668; -.
DR STRING; 9606.ENSP00000342962; -.
DR PhosphoSite; Q9NRX5; -.
DR DMDM; 25453298; -.
DR PaxDb; Q9NRX5; -.
DR PRIDE; Q9NRX5; -.
DR DNASU; 57515; -.
DR Ensembl; ENST00000339697; ENSP00000342962; ENSG00000111897.
DR Ensembl; ENST00000368454; ENSP00000357439; ENSG00000111897.
DR GeneID; 57515; -.
DR KEGG; hsa:57515; -.
DR UCSC; uc003pyy.1; human.
DR CTD; 57515; -.
DR GeneCards; GC06M122807; -.
DR HGNC; HGNC:13464; SERINC1.
DR HPA; HPA035738; -.
DR HPA; HPA035739; -.
DR MIM; 614548; gene.
DR neXtProt; NX_Q9NRX5; -.
DR PharmGKB; PA134973249; -.
DR eggNOG; NOG308011; -.
DR HOVERGEN; HBG025699; -.
DR InParanoid; Q9NRX5; -.
DR OMA; SKWPSVW; -.
DR OrthoDB; EOG7TXKGQ; -.
DR PhylomeDB; Q9NRX5; -.
DR ChiTaRS; SERINC1; human.
DR GeneWiki; SERINC1; -.
DR GenomeRNAi; 57515; -.
DR NextBio; 63885; -.
DR PRO; PR:Q9NRX5; -.
DR Bgee; Q9NRX5; -.
DR CleanEx; HS_SERINC1; -.
DR Genevestigator; Q9NRX5; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; ISS:HGNC.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:HGNC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051347; P:positive regulation of transferase activity; ISS:HGNC.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:HGNC.
DR InterPro; IPR005016; TMS_TDE.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR Pfam; PF03348; Serinc; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane;
KW Myristate; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 453 Serine incorporator 1.
FT /FTId=PRO_0000218966.
FT TOPO_DOM 2 39 Cytoplasmic (Potential).
FT TRANSMEM 40 60 Helical; (Potential).
FT TOPO_DOM 61 88 Lumenal (Potential).
FT TRANSMEM 89 109 Helical; (Potential).
FT TOPO_DOM 110 123 Cytoplasmic (Potential).
FT TRANSMEM 124 144 Helical; (Potential).
FT TOPO_DOM 145 151 Lumenal (Potential).
FT TRANSMEM 152 172 Helical; (Potential).
FT TOPO_DOM 173 197 Cytoplasmic (Potential).
FT TRANSMEM 198 218 Helical; (Potential).
FT TOPO_DOM 219 231 Lumenal (Potential).
FT TRANSMEM 232 252 Helical; (Potential).
FT TOPO_DOM 253 259 Cytoplasmic (Potential).
FT TRANSMEM 260 280 Helical; (Potential).
FT TOPO_DOM 281 309 Lumenal (Potential).
FT TRANSMEM 310 330 Helical; (Potential).
FT TOPO_DOM 331 387 Cytoplasmic (Potential).
FT TRANSMEM 388 408 Helical; (Potential).
FT TOPO_DOM 409 426 Lumenal (Potential).
FT TRANSMEM 427 447 Helical; (Potential).
FT TOPO_DOM 448 453 Cytoplasmic (Potential).
FT MOD_RES 351 351 Phosphoserine.
FT MOD_RES 352 352 Phosphothreonine.
FT MOD_RES 361 361 Phosphoserine.
FT MOD_RES 364 364 Phosphoserine.
FT LIPID 2 2 N-myristoyl glycine.
FT CARBOHYD 298 298 N-linked (GlcNAc...).
FT VARIANT 199 199 L -> V (in dbSNP:rs13210569).
FT /FTId=VAR_052275.
FT VARIANT 216 216 F -> V (in dbSNP:rs13210446).
FT /FTId=VAR_052276.
FT VARIANT 225 225 S -> G (in dbSNP:rs17260829).
FT /FTId=VAR_052277.
FT CONFLICT 89 89 A -> S (in Ref. 9; AAH28607).
FT CONFLICT 247 247 S -> F (in Ref. 1; AAP97200/AAP97211).
FT CONFLICT 408 408 Y -> S (in Ref. 5; AAQ88795).
SQ SEQUENCE 453 AA; 50495 MW; 3868DBF38165B78C CRC64;
MGSVLGLCSM ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG
MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA
VHNGFWFFKF AAAIAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE
SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAIVLFFVYY THPASCSENK AFISVNMLLC
VGASVMSILP KIQESQPRSG LLQSSVITVY TMYLTWSAMT NEPETNCNPS LLSIIGYNTT
STVPKEGQSV QWWHAQGIIG LILFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGGAR
SDGSLEDGDD VHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
TAVWVKISSS WIGIVLYVWT LVAPLVLTNR DFD
//
MIM
614548
*RECORD*
*FIELD* NO
614548
*FIELD* TI
*614548 SERINE INCORPORATOR 1; SERINC1
;;TMS2;;
KIAA1253
*FIELD* TX
DESCRIPTION
SERINC1 belongs to the SERINC family of transmembrane proteins that
read morefacilitate incorporation of serine into phosphatidylserine and
sphingolipids (Inuzuka et al., 2005).
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1999) cloned SERINC1, which they designated
KIAA1253. RT-PCR ELISA detected SERINC1 expression in all adult and
fetal tissues and adult brain regions examined. Highest expression was
in brain, predominantly in caudate nucleus, and lowest expression was in
pancreas, spleen, and testis.
Grossman et al. (2000) cloned mouse Serinc1, which they called Tms2, and
they identified human TMS2 by database analysis. The deduced mouse and
human proteins contain 453 and 440 amino acids, respectively. Both have
11 transmembrane segments, a MYC (190080)-type helix-loop-helix
dimerization motif between transmembrane domains 7 and 8, and several
putative phosphorylation sites. In situ hybridization of mouse brain
revealed Tms2 expression in virtually every neuron, with highest
expression in hippocampus, olfactory bulb, cerebral cortex, and granule
cell layer of cerebellum. No Tms2 expression was detected in peripheral
tissues. Epitope-tagged Tms2 was expressed in a punctate distribution on
the surface of transfected HEK293 cells.
Inuzuka et al. (2005) found that rat Serinc1 was expressed in
endoplasmic reticulum (ER) membranes of transfected COS cells.
GENE FUNCTION
Inuzuka et al. (2005) found that Serinc1 mRNA was upregulated in rat
hippocampal CA1-3 neurons following kainate-induced seizure. Expression
of rat Serinc1 in E. coli, yeast, or COS cells enhanced the activity of
phosphatidylserine synthase (see 612792), resulting in enhanced
incorporation of radiolabeled serine into phosphatidylserine. Serinc1
did not enhance serine uptake. In COS cells, Serinc1 also enhanced the
activity of serine palmitoyltransferase (see 605712), resulting in
incorporation of serine into 3-ketodihydrosphingosine. Serinc1 and
serine palmitoyltransferase colocalized at ER membranes, and yeast
2-hybrid experiments revealed that the 2 proteins interacted directly.
MAPPING
Hartz (2012) mapped the SERINC1 gene to chromosome 6q22.31 based on an
alignment of the SERINC1 sequence (GenBank GENBANK AB033079) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Grossman, T. R.; Luque, J. M.; Nelson, N.: Identification of a
ubiquitous family of membrane proteins and their expression in mouse
brain. J. Exp. Biol. 203: 447-457, 2000.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/3/2012.
3. Inuzuka, M.; Hayakawa, M.; Ingi, T.: Serinc, an activity-regulated
protein family, incorporates serine into membrane lipid synthesis. J.
Biol. Chem. 280: 35776-35783, 2005.
4. Nagase, T.; Ishikawa, K.; Kikuno, R.; Hirosawa, M.; Nomura, N.;
Ohara, O.: Prediction of the coding sequences of unidentified human
genes. XV. The complete sequences of 100 new cDNA clones from brain
which code for large proteins in vitro. DNA Res. 6: 337-345, 1999.
*FIELD* CD
Patricia A. Hartz: 3/23/2012
*FIELD* ED
mgross: 03/23/2012
*RECORD*
*FIELD* NO
614548
*FIELD* TI
*614548 SERINE INCORPORATOR 1; SERINC1
;;TMS2;;
KIAA1253
*FIELD* TX
DESCRIPTION
SERINC1 belongs to the SERINC family of transmembrane proteins that
read morefacilitate incorporation of serine into phosphatidylserine and
sphingolipids (Inuzuka et al., 2005).
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1999) cloned SERINC1, which they designated
KIAA1253. RT-PCR ELISA detected SERINC1 expression in all adult and
fetal tissues and adult brain regions examined. Highest expression was
in brain, predominantly in caudate nucleus, and lowest expression was in
pancreas, spleen, and testis.
Grossman et al. (2000) cloned mouse Serinc1, which they called Tms2, and
they identified human TMS2 by database analysis. The deduced mouse and
human proteins contain 453 and 440 amino acids, respectively. Both have
11 transmembrane segments, a MYC (190080)-type helix-loop-helix
dimerization motif between transmembrane domains 7 and 8, and several
putative phosphorylation sites. In situ hybridization of mouse brain
revealed Tms2 expression in virtually every neuron, with highest
expression in hippocampus, olfactory bulb, cerebral cortex, and granule
cell layer of cerebellum. No Tms2 expression was detected in peripheral
tissues. Epitope-tagged Tms2 was expressed in a punctate distribution on
the surface of transfected HEK293 cells.
Inuzuka et al. (2005) found that rat Serinc1 was expressed in
endoplasmic reticulum (ER) membranes of transfected COS cells.
GENE FUNCTION
Inuzuka et al. (2005) found that Serinc1 mRNA was upregulated in rat
hippocampal CA1-3 neurons following kainate-induced seizure. Expression
of rat Serinc1 in E. coli, yeast, or COS cells enhanced the activity of
phosphatidylserine synthase (see 612792), resulting in enhanced
incorporation of radiolabeled serine into phosphatidylserine. Serinc1
did not enhance serine uptake. In COS cells, Serinc1 also enhanced the
activity of serine palmitoyltransferase (see 605712), resulting in
incorporation of serine into 3-ketodihydrosphingosine. Serinc1 and
serine palmitoyltransferase colocalized at ER membranes, and yeast
2-hybrid experiments revealed that the 2 proteins interacted directly.
MAPPING
Hartz (2012) mapped the SERINC1 gene to chromosome 6q22.31 based on an
alignment of the SERINC1 sequence (GenBank GENBANK AB033079) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Grossman, T. R.; Luque, J. M.; Nelson, N.: Identification of a
ubiquitous family of membrane proteins and their expression in mouse
brain. J. Exp. Biol. 203: 447-457, 2000.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/3/2012.
3. Inuzuka, M.; Hayakawa, M.; Ingi, T.: Serinc, an activity-regulated
protein family, incorporates serine into membrane lipid synthesis. J.
Biol. Chem. 280: 35776-35783, 2005.
4. Nagase, T.; Ishikawa, K.; Kikuno, R.; Hirosawa, M.; Nomura, N.;
Ohara, O.: Prediction of the coding sequences of unidentified human
genes. XV. The complete sequences of 100 new cDNA clones from brain
which code for large proteins in vitro. DNA Res. 6: 337-345, 1999.
*FIELD* CD
Patricia A. Hartz: 3/23/2012
*FIELD* ED
mgross: 03/23/2012