SERC4_HUMAN
ID SERC4_HUMAN Reviewed; 518 AA.
AC A6NH21; B2RN41; Q3YL75;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Serine incorporator 4;
GN Name=SERINC4;
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 2), AND FUNCTION.
RC TISSUE=Lung;
RX PubMed=16120614; DOI=10.1074/jbc.m505712200;
RA Inuzuka M., Hayakawa M., Ingi T.;
RT "Serinc, an activity-regulated protein family, incorporates serine into
RT membrane lipid synthesis.";
RL J. Biol. Chem. 280:35776-35783(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Incorporates a polar amino acid serine into membranes and
CC facilitates the synthesis of two serine-derived lipids,
CC phosphatidylserine and sphingolipids. {ECO:0000269|PubMed:16120614}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6NH21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NH21-2; Sequence=VSP_033584, VSP_033585;
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; DQ103711; AAZ80298.1; -; mRNA.
DR EMBL; AC018512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77244.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77245.1; -; Genomic_DNA.
DR EMBL; BC136669; AAI36670.1; -; mRNA.
DR CCDS; CCDS58360.1; -. [A6NH21-1]
DR RefSeq; NP_001244960.1; NM_001258031.1. [A6NH21-1]
DR RefSeq; NP_001244961.1; NM_001258032.1. [A6NH21-2]
DR AlphaFoldDB; A6NH21; -.
DR SMR; A6NH21; -.
DR STRING; 9606.ENSP00000319796; -.
DR iPTMnet; A6NH21; -.
DR PhosphoSitePlus; A6NH21; -.
DR BioMuta; SERINC4; -.
DR MassIVE; A6NH21; -.
DR PaxDb; A6NH21; -.
DR PeptideAtlas; A6NH21; -.
DR PRIDE; A6NH21; -.
DR Antibodypedia; 11477; 54 antibodies from 16 providers.
DR DNASU; 619189; -.
DR Ensembl; ENST00000319327.7; ENSP00000319796.6; ENSG00000184716.14. [A6NH21-1]
DR GeneID; 619189; -.
DR KEGG; hsa:619189; -.
DR MANE-Select; ENST00000319327.7; ENSP00000319796.6; NM_001258031.2; NP_001244960.1.
DR UCSC; uc031qrp.2; human. [A6NH21-1]
DR CTD; 619189; -.
DR GeneCards; SERINC4; -.
DR HGNC; HGNC:32237; SERINC4.
DR HPA; ENSG00000184716; Tissue enriched (retina).
DR MIM; 614550; gene.
DR neXtProt; NX_A6NH21; -.
DR PharmGKB; PA142670936; -.
DR VEuPathDB; HostDB:ENSG00000184716; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_2_1; -.
DR InParanoid; A6NH21; -.
DR OMA; IHNFWFL; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; A6NH21; -.
DR TreeFam; TF312881; -.
DR PathwayCommons; A6NH21; -.
DR Reactome; R-HSA-977347; Serine biosynthesis.
DR BioGRID-ORCS; 619189; 42 hits in 1061 CRISPR screens.
DR ChiTaRS; SERINC4; human.
DR GenomeRNAi; 619189; -.
DR Pharos; A6NH21; Tdark.
DR PRO; PR:A6NH21; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; A6NH21; protein.
DR Bgee; ENSG00000184716; Expressed in thymus and 57 other tissues.
DR ExpressionAtlas; A6NH21; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR029563; Serinc4.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF5; PTHR10383:SF5; 1.
DR Pfam; PF03348; Serinc; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Serine incorporator 4"
FT /id="PRO_0000333871"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16120614"
FT /id="VSP_033584"
FT VAR_SEQ 245..282
FT /note="HYYTHPAGCLLNKMLLSLHLCFCGLISFLSIAPCIRLK -> MSISSQHGIT
FT LASVEALHSSYCSWCLLQLLPIPGTRTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16120614"
FT /id="VSP_033585"
SQ SEQUENCE 518 AA; 56870 MW; 93A6224C102565AE CRC64;
MVGAKAGPSP GTSLGLAQQH SGGSSVLVKS PFCQVCCCGP APCASCCHSR WPSLTASTCS
RLFYILLHVG ASAICCLLLS RTVVERVWGK THRIQMPSGL CAHLFGLSDC PVLSGSGAVY
RVCAGTATFH LLQAVLLVHL HSPTSPRAQL HNSFWLLKLL FLLGLCAIAF CIPDEHLFPA
WHYIGICGGF AFILLQLVLI TAFAHSWNKN WQTGAAQDCS WFLAVLLATL GFYSMAGVGA
VLLFHYYTHP AGCLLNKMLL SLHLCFCGLI SFLSIAPCIR LKQPRSGLLQ ASVISCYIMY
LTFSALSSRP PERVILQGQN HTLCLPGLSK MEPQTPDISL AMLSASIMYA CVLFACNEAS
YLAEVFGPLW IVKVYSYEFQ KPSLCFCCPE TVEADKGQRG GAARPADQET PPAPPVQVQH
LSYNYSAFHF VFFLASLYVM VTLTNWFSYE GAELEKTFIK GSWATFWVKV ASCWACVLLY
LGLLLAPLCW PPTQKPQPLI LRRRRHRIIS PDNKYPPV
