GenomeNet

Database: UniProt
Entry: Q14162
LinkDB: Q14162
Original site: Q14162 
ID   SREC_HUMAN              Reviewed;         830 AA.
AC   Q14162; A8MQ05; O43701; Q8NHD2; Q8NHD3; Q8NHD4; Q8NHD5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   10-APR-2019, entry version 168.
DE   RecName: Full=Scavenger receptor class F member 1;
DE   AltName: Full=Acetyl LDL receptor;
DE   AltName: Full=Scavenger receptor expressed by endothelial cells 1;
DE            Short=SREC-I;
DE   Flags: Precursor;
GN   Name=SCARF1; Synonyms=KIAA0149, SREC;
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], AND VARIANTS VAL-425; ASP-639; TRP-662 AND
RP   SER-667.
RC   TISSUE=Umbilical vein endothelial cell;
RX   PubMed=9395444; DOI=10.1074/jbc.272.50.31217;
RA   Adachi H., Tsujimoto M., Arai H., Inoue K.;
RT   "Expression cloning of a novel scavenger receptor from human
RT   endothelial cells.";
RL   J. Biol. Chem. 272:31217-31220(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND VARIANTS VAL-425; ASP-639 AND
RP   SER-667.
RC   TISSUE=Peripheral blood leukocyte;
RX   PubMed=11978792; DOI=10.1074/jbc.M201854200;
RA   Adachi H., Tsujimoto M.;
RT   "Characterization of the human gene encoding the scavenger receptor
RT   expressed by endothelial cell and its regulation by a novel
RT   transcription factor, endothelial zinc finger protein-2.";
RL   J. Biol. Chem. 277:24014-24021(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-425; ASP-639;
RP   TRP-662 AND SER-667.
RC   TISSUE=Bone marrow;
RX   PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA   Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. IV.
RT   The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT   analysis of cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:167-174(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-425.
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-425; ASP-639
RP   AND SER-667.
RC   TISSUE=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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Mediates the binding and degradation of acetylated low
CC       density lipoprotein (Ac-LDL). Mediates heterophilic interactions,
CC       suggesting a function as adhesion protein. Plays a role in the
CC       regulation of neurite-like outgrowth (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterophilic interaction with SREC2 via its extracellular
CC       domain. The heterophilic interaction is suppressed by the presence
CC       of ligand such as Ac-LDL. Interacts with AVIL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=SREC-1;
CC         IsoId=Q14162-1; Sequence=Displayed;
CC       Name=2; Synonyms=SREC-5;
CC         IsoId=Q14162-2; Sequence=VSP_039956;
CC       Name=3; Synonyms=SREC-3;
CC         IsoId=Q14162-3; Sequence=VSP_039960, VSP_039961;
CC       Name=4; Synonyms=SREC-4;
CC         IsoId=Q14162-4; Sequence=VSP_039957;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
CC       Name=5; Synonyms=SREC-2;
CC         IsoId=Q14162-5; Sequence=VSP_039958, VSP_039959;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Endothelial cells.
DR   EMBL; D86864; BAA24070.1; -; mRNA.
DR   EMBL; AB052946; BAC02692.1; -; Genomic_DNA.
DR   EMBL; AB052947; BAC02693.1; -; mRNA.
DR   EMBL; AB052948; BAC02694.1; -; mRNA.
DR   EMBL; AB052949; BAC02695.1; -; mRNA.
DR   EMBL; AB052950; BAC02696.1; -; mRNA.
DR   EMBL; D63483; BAA09770.1; -; mRNA.
DR   EMBL; AC130343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90596.1; -; Genomic_DNA.
DR   EMBL; BC039735; AAH39735.1; -; mRNA.
DR   CCDS; CCDS11007.1; -. [Q14162-1]
DR   CCDS; CCDS45564.1; -. [Q14162-3]
DR   RefSeq; NP_003684.2; NM_003693.3. [Q14162-1]
DR   RefSeq; NP_663325.1; NM_145350.2. [Q14162-3]
DR   UniGene; Hs.647430; -.
DR   ProteinModelPortal; Q14162; -.
DR   SMR; Q14162; -.
DR   IntAct; Q14162; 17.
DR   STRING; 9606.ENSP00000263071; -.
DR   iPTMnet; Q14162; -.
DR   PhosphoSitePlus; Q14162; -.
DR   SwissPalm; Q14162; -.
DR   BioMuta; SCARF1; -.
DR   DMDM; 311033530; -.
DR   jPOST; Q14162; -.
DR   PaxDb; Q14162; -.
DR   PeptideAtlas; Q14162; -.
DR   PRIDE; Q14162; -.
DR   ProteomicsDB; 59887; -.
DR   ProteomicsDB; 59888; -. [Q14162-2]
DR   ProteomicsDB; 59889; -. [Q14162-3]
DR   ProteomicsDB; 59890; -. [Q14162-4]
DR   ProteomicsDB; 59891; -. [Q14162-5]
DR   Ensembl; ENST00000263071; ENSP00000263071; ENSG00000074660. [Q14162-1]
DR   Ensembl; ENST00000434376; ENSP00000411167; ENSG00000074660. [Q14162-5]
DR   Ensembl; ENST00000571272; ENSP00000458174; ENSG00000074660. [Q14162-3]
DR   Ensembl; ENST00000621348; ENSP00000481595; ENSG00000276336. [Q14162-1]
DR   Ensembl; ENST00000631462; ENSP00000487665; ENSG00000276336. [Q14162-5]
DR   Ensembl; ENST00000632317; ENSP00000488776; ENSG00000276336. [Q14162-3]
DR   GeneID; 8578; -.
DR   KEGG; hsa:8578; -.
DR   UCSC; uc002fsy.3; human. [Q14162-1]
DR   CTD; 8578; -.
DR   EuPathDB; HostDB:ENSG00000074660.15; -.
DR   GeneCards; SCARF1; -.
DR   H-InvDB; HIX0013404; -.
DR   HGNC; HGNC:16820; SCARF1.
DR   HPA; HPA072936; -.
DR   MIM; 607873; gene.
DR   neXtProt; NX_Q14162; -.
DR   OpenTargets; ENSG00000074660; -.
DR   PharmGKB; PA38420; -.
DR   eggNOG; KOG1218; Eukaryota.
DR   eggNOG; ENOG410XQWV; LUCA.
DR   GeneTree; ENSGT00950000183101; -.
DR   HOGENOM; HOG000015093; -.
DR   HOVERGEN; HBG099941; -.
DR   InParanoid; Q14162; -.
DR   OMA; CVPPQEG; -.
DR   OrthoDB; 110992at2759; -.
DR   PhylomeDB; Q14162; -.
DR   TreeFam; TF332598; -.
DR   Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
DR   GenomeRNAi; 8578; -.
DR   PRO; PR:Q14162; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000074660; Expressed in 159 organ(s), highest expression level in spleen.
DR   ExpressionAtlas; Q14162; baseline and differential.
DR   Genevisible; Q14162; HS.
DR   GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006707; P:cholesterol catabolic process; IC:UniProtKB.
DR   GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR   GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB.
DR   GO; GO:0048680; P:positive regulation of axon regeneration; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR033329; SCARF1.
DR   PANTHER; PTHR24043:SF0; PTHR24043:SF0; 1.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   SMART; SM00181; EGF; 9.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    830       Scavenger receptor class F member 1.
FT                                /FTId=PRO_0000007738.
FT   TOPO_DOM     20    421       Extracellular. {ECO:0000255}.
FT   TRANSMEM    422    442       Helical. {ECO:0000255}.
FT   TOPO_DOM    443    830       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       53     87       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       95    130       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      155    191       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      215    249       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      302    339       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      351    382       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    431    438       Poly-Leu.
FT   COMPBIAS    476    620       Pro/Ser-rich.
FT   COMPBIAS    622    798       Gly-rich.
FT   MOD_RES     589    589       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5ND28}.
FT   MOD_RES     606    606       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   CARBOHYD    289    289       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    382    382       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    393    393       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57     69       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     63     75       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     77     86       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     99    111       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    105    118       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    120    129       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    159    172       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    165    179       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    181    190       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    219    230       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    225    237       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    239    248       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    306    319       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    313    326       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    329    338       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    355    363       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    358    370       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    372    381       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     330    415       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11978792}.
FT                                /FTId=VSP_039956.
FT   VAR_SEQ     338    830       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:11978792}.
FT                                /FTId=VSP_039957.
FT   VAR_SEQ     338    342       CEDPC -> GPVIL (in isoform 5).
FT                                {ECO:0000303|PubMed:11978792}.
FT                                /FTId=VSP_039958.
FT   VAR_SEQ     343    830       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:11978792}.
FT                                /FTId=VSP_039959.
FT   VAR_SEQ     496    569       VSHHDPEVPFNHSFIEPPSAGWATDDSFSSDPESGEADEVP
FT                                AYCVPPQEGMVPVAQAGSSEASLAAGAFPPPED -> ASSS
FT                                RPLPAGPLMTPSHPILSLERQMRFLPTVCHPKKGWSLWPRQ
FT                                GRQRPAWLQVLSRPLRTPPRHSPSRAPPA (in isoform
FT                                3). {ECO:0000303|PubMed:11978792}.
FT                                /FTId=VSP_039960.
FT   VAR_SEQ     570    830       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11978792}.
FT                                /FTId=VSP_039961.
FT   VARIANT     425    425       A -> V (in dbSNP:rs2272011).
FT                                {ECO:0000269|PubMed:11978792,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8590280,
FT                                ECO:0000269|PubMed:9395444,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_047249.
FT   VARIANT     618    618       R -> K (in dbSNP:rs35455643).
FT                                /FTId=VAR_047250.
FT   VARIANT     639    639       E -> D (in dbSNP:rs3744644).
FT                                {ECO:0000269|PubMed:11978792,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8590280,
FT                                ECO:0000269|PubMed:9395444}.
FT                                /FTId=VAR_047251.
FT   VARIANT     662    662       R -> W (in dbSNP:rs8072430).
FT                                {ECO:0000269|PubMed:8590280,
FT                                ECO:0000269|PubMed:9395444}.
FT                                /FTId=VAR_047252.
FT   VARIANT     667    667       G -> S (in dbSNP:rs4790250).
FT                                {ECO:0000269|PubMed:11978792,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8590280,
FT                                ECO:0000269|PubMed:9395444}.
FT                                /FTId=VAR_047253.
FT   VARIANT     748    748       G -> V (in dbSNP:rs3760460).
FT                                /FTId=VAR_047254.
FT   CONFLICT    328    329       RC -> PG (in Ref. 2; BAC02696).
FT                                {ECO:0000305}.
SQ   SEQUENCE   830 AA;  87387 MW;  3D1CBF0D6F2BA055 CRC64;
     MGLGLLLPLL LLWTRGTQGS ELDPKGQHVC VASSPSAELQ CCAGWRQKDQ ECTIPICEGP
     DACQKDEVCV KPGLCRCKPG FFGAHCSSRC PGQYWGPDCR ESCPCHPHGQ CEPATGACQC
     QADRWGARCE FPCACGPHGR CDPATGVCHC EPGWWSSTCR RPCQCNTAAA RCEQATGACV
     CKPGWWGRRC SFRCNCHGSP CEQDSGRCAC RPGWWGPECQ QQCECVRGRC SAASGECTCP
     PGFRGARCEL PCPAGSHGVQ CAHSCGRCKH NEPCSPDTGS CESCEPGWNG TQCQQPCLPG
     TFGESCEQQC PHCRHGEACE PDTGHCQRCD PGWLGPRCED PCPTGTFGED CGSTCPTCVQ
     GSCDTVTGDC VCSAGYWGPS CNASCPAGFH GNNCSVPCEC PEGLCHPVSG SCQPGSGSRD
     TALIAGSLVP LLLLFLGLAC CACCCWAPRS DLKDRPARDG ATVSRMKLQV WGTLTSLGST
     LPCRSLSSHK LPWVTVSHHD PEVPFNHSFI EPPSAGWATD DSFSSDPESG EADEVPAYCV
     PPQEGMVPVA QAGSSEASLA AGAFPPPEDA STPFAIPRTS SLARAKRPSV SFAEGTKFAP
     QSRRSSGELS SPLRKPKRLS RGAQSGPEGR EAEESTGPEE AEAPESFPAA ASPGDSATGH
     RRPPLGGRTV AEHVEAIEGS VQESSGPVTT IYMLAGKPRG SEGPVRSVFR HFGSFQKGQA
     EAKVKRAIPK PPRQALNRKK GSPGLASGSV GQSPNSAPKA GLPGATGPMA VRPEEAVRGL
     GAGTESSRRA QEPVSGCGSP EQDPQKQAEE ERQEEPEYEN VVPISRPPEP
//
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