SERC5_HUMAN
ID SERC5_HUMAN Reviewed; 423 AA.
AC Q86VE9; B4DMH7; Q495A4; Q495A6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Serine incorporator 5 {ECO:0000305};
GN Name=SERINC5 {ECO:0000312|HGNC:HGNC:18825}; Synonyms=C5orf12;
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] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetus;
RX PubMed=12688535; DOI=10.1023/a:1022250428015;
RA Xu J., Ji C., Wang L., Cao Y., Dai J., Ye X., Zeng L., Dai J., Wu Q.,
RA Xie Y., Mao Y.;
RT "Cloning and expression of a novel human C5orf12 gene, a member of the
RT TMS_TDE family.";
RL Mol. Biol. Rep. 30:47-52(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBCELLULAR LOCATION (MICROBIAL
RP INFECTION).
RX PubMed=26416733; DOI=10.1038/nature15400;
RA Usami Y., Wu Y., Goettlinger H.G.;
RT "SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by
RT Nef.";
RL Nature 526:218-223(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBCELLULAR LOCATION (MICROBIAL
RP INFECTION).
RX PubMed=26416734; DOI=10.1038/nature15399;
RA Rosa A., Chande A., Ziglio S., De Sanctis V., Bertorelli R., Goh S.L.,
RA McCauley S.M., Nowosielska A., Antonarakis S.E., Luban J., Santoni F.A.,
RA Pizzato M.;
RT "HIV-1 Nef promotes infection by excluding SERINC5 from virion
RT incorporation.";
RL Nature 526:212-217(2015).
CC -!- FUNCTION: Restriction factor required to restrict infectivity of
CC lentiviruses, such as HIV-1: acts by inhibiting an early step of viral
CC infection. Impairs the penetration of the viral particle into the
CC cytoplasm (PubMed:26416733, PubMed:26416734). Enhances the
CC incorporation of serine into phosphatidylserine and sphingolipids. May
CC play a role in providing serine molecules for the formation of myelin
CC glycosphingolipids in oligodendrocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q63175, ECO:0000269|PubMed:26416733,
CC ECO:0000269|PubMed:26416734}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26416733,
CC ECO:0000269|PubMed:26416734}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}.
CC Note=(Microbial infection) Upon HIV-1 infection, it is redirected to
CC perinuclear region following interaction with HIV-1 Nef, excluding it
CC from virions particles, thereby preventing subsequent antiviral defense
CC activity (PubMed:26416733, PubMed:26416734). Localizes to the cell
CC membrane, where it is efficiently incorporated into budding virions and
CC impairs subsequent virion entry into target cells (PubMed:26416733,
CC PubMed:26416734). {ECO:0000269|PubMed:26416734,
CC ECO:0000305|PubMed:26416733}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86VE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VE9-2; Sequence=VSP_033055;
CC Name=3;
CC IsoId=Q86VE9-3; Sequence=VSP_033054;
CC Name=4;
CC IsoId=Q86VE9-4; Sequence=VSP_042310;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, skeletal muscle,
CC spleen, thymus, testis and peripheral leukocyte and is expressed weakly
CC in the heart, liver and fetal brain. {ECO:0000269|PubMed:12688535}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; AF498273; AAP06800.1; -; mRNA.
DR EMBL; AK297467; BAG59889.1; -; mRNA.
DR EMBL; AC010260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95843.1; -; Genomic_DNA.
DR EMBL; CH471084; EAW95844.1; -; Genomic_DNA.
DR EMBL; CH471084; EAW95845.1; -; Genomic_DNA.
DR EMBL; BC101280; AAI01281.1; -; mRNA.
DR EMBL; BC101281; AAI01282.1; -; mRNA.
DR EMBL; BC101283; AAI01284.1; -; mRNA.
DR CCDS; CCDS54874.1; -. [Q86VE9-4]
DR CCDS; CCDS83009.1; -. [Q86VE9-2]
DR RefSeq; NP_001167542.1; NM_001174071.2. [Q86VE9-2]
DR RefSeq; NP_001167543.1; NM_001174072.2. [Q86VE9-4]
DR RefSeq; NP_840060.1; NM_178276.6. [Q86VE9-1]
DR AlphaFoldDB; Q86VE9; -.
DR SMR; Q86VE9; -.
DR BioGRID; 129188; 4.
DR DIP; DIP-47313N; -.
DR IntAct; Q86VE9; 2.
DR MINT; Q86VE9; -.
DR STRING; 9606.ENSP00000426237; -.
DR TCDB; 9.A.29.3.5; the lantibiotic immunity protein/serine connector (lip/sip) family.
DR GlyGen; Q86VE9; 2 sites.
DR iPTMnet; Q86VE9; -.
DR PhosphoSitePlus; Q86VE9; -.
DR BioMuta; SERINC5; -.
DR DMDM; 74714045; -.
DR EPD; Q86VE9; -.
DR jPOST; Q86VE9; -.
DR MassIVE; Q86VE9; -.
DR MaxQB; Q86VE9; -.
DR PaxDb; Q86VE9; -.
DR PeptideAtlas; Q86VE9; -.
DR PRIDE; Q86VE9; -.
DR ProteomicsDB; 69993; -. [Q86VE9-1]
DR ProteomicsDB; 69994; -. [Q86VE9-2]
DR ProteomicsDB; 69995; -. [Q86VE9-3]
DR ProteomicsDB; 69996; -. [Q86VE9-4]
DR Antibodypedia; 49006; 22 antibodies from 8 providers.
DR DNASU; 256987; -.
DR Ensembl; ENST00000507668.7; ENSP00000426237.3; ENSG00000164300.17. [Q86VE9-4]
DR Ensembl; ENST00000509193.5; ENSP00000426134.2; ENSG00000164300.17. [Q86VE9-2]
DR Ensembl; ENST00000512972.6; ENSP00000421665.2; ENSG00000164300.17. [Q86VE9-3]
DR GeneID; 256987; -.
DR KEGG; hsa:256987; -.
DR MANE-Select; ENST00000507668.7; ENSP00000426237.3; NM_001174072.3; NP_001167543.1. [Q86VE9-4]
DR UCSC; uc011ctj.2; human. [Q86VE9-1]
DR CTD; 256987; -.
DR DisGeNET; 256987; -.
DR GeneCards; SERINC5; -.
DR HGNC; HGNC:18825; SERINC5.
DR HPA; ENSG00000164300; Low tissue specificity.
DR MIM; 614551; gene.
DR neXtProt; NX_Q86VE9; -.
DR OpenTargets; ENSG00000164300; -.
DR PharmGKB; PA38698; -.
DR VEuPathDB; HostDB:ENSG00000164300; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_2_1; -.
DR InParanoid; Q86VE9; -.
DR OMA; ASCWVCV; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q86VE9; -.
DR TreeFam; TF312881; -.
DR PathwayCommons; Q86VE9; -.
DR Reactome; R-HSA-977347; Serine biosynthesis.
DR SignaLink; Q86VE9; -.
DR BioGRID-ORCS; 256987; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; SERINC5; human.
DR GenomeRNAi; 256987; -.
DR Pharos; Q86VE9; Tbio.
DR PRO; PR:Q86VE9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86VE9; protein.
DR Bgee; ENSG00000164300; Expressed in tibia and 204 other tissues.
DR ExpressionAtlas; Q86VE9; baseline and differential.
DR Genevisible; Q86VE9; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0009597; P:detection of virus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; TAS:Reactome.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:HGNC-UCL.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1904219; P:positive regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity; ISS:HGNC.
DR GO; GO:1904222; P:positive regulation of serine C-palmitoyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR InterPro; IPR029555; Serinc5.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF16; PTHR10383:SF16; 1.
DR Pfam; PF03348; Serinc; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antiviral defense; Cell membrane; Cytoplasm;
KW Glycoprotein; Host-virus interaction; Immunity; Innate immunity;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..423
FT /note="Serine incorporator 5"
FT /id="PRO_0000330630"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 413..423
FT /note="NHVRSAFHLLP -> KNYQC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033054"
FT VAR_SEQ 413..416
FT /note="NHVR -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033055"
FT VAR_SEQ 414..423
FT /note="HVRSAFHLLP -> YESANIESFFSGSWSIFWVKMASCWICVLLYLCTLVAP
FT LCCPTREFSV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042310"
SQ SEQUENCE 423 AA; 47009 MW; B05A461D418D049B CRC64;
MSAQCCAGQL ACCCGSAGCS LCCDCCPRIR QSLSTRFMYA LYFILVVVLC CIMMSTTVAH
KMKEHIPFFE DMCKGIKAGD TCEKLVGYSA VYRVCFGMAC FFFIFCLLTL KINNSKSCRA
HIHNGFWFFK LLLLGAMCSG AFFIPDQDTF LNAWRYVGAV GGFLFIGIQL LLLVEFAHKW
NKNWTAGTAS NKLWYASLAL VTLIMYSIAT GGLVLMAVFY TQKDSCMENK ILLGVNGGLC
LLISLVAISP WVQNRQPHSG LLQSGVISCY VTYLTFSALS SKPAEVVLDE HGKNVTICVP
DFGQDLYRDE NLVTILGTSL LIGCILYSCL TSTTRSSSDA LQGRYAAPEL EIARCCFCFS
PGGEDTEEQQ PGKEGPRVIY DEKKGTVYIY SYFHFVFFLA SLYVMMTVTN WFNHVRSAFH
LLP
