SREC_HUMAN
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 03-AUG-2022, entry version 186.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 endothelial
RT cells.";
RL J. Biol. Chem. 272:31217-31220(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA]
RP (ISOFORMS 2; 3; 4 AND 5), AND VARIANTS VAL-425; ASP-639 AND 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 transcription
RT 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. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT 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., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., 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 the
RT 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., 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-425; ASP-639 AND
RP 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 project:
RT 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 BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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). {ECO:0000250}.
CC -!- SUBUNIT: Heterophilic interaction with SREC2 via its extracellular
CC domain. The heterophilic interaction is suppressed by the presence of
CC ligand such as Ac-LDL. Interacts with AVIL (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q14162; O95471: CLDN7; NbExp=3; IntAct=EBI-12056025, EBI-740744;
CC Q14162; O75208: COQ9; NbExp=3; IntAct=EBI-12056025, EBI-724524;
CC Q14162; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12056025, EBI-6942903;
CC Q14162; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12056025, EBI-3867333;
CC Q14162; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12056025, EBI-18304435;
CC Q14162; P48165: GJA8; NbExp=3; IntAct=EBI-12056025, EBI-17458373;
CC Q14162; O60883: GPR37L1; NbExp=3; IntAct=EBI-12056025, EBI-2927498;
CC Q14162; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12056025, EBI-11721746;
CC Q14162; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-12056025, EBI-18053395;
CC Q14162; P48051: KCNJ6; NbExp=3; IntAct=EBI-12056025, EBI-12017638;
CC Q14162; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-12056025, EBI-11959885;
CC Q14162; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12056025, EBI-10171774;
CC Q14162; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-12056025, EBI-11987425;
CC Q14162; Q5T752: LCE1D; NbExp=3; IntAct=EBI-12056025, EBI-11741311;
CC Q14162; Q6ZUX7: LHFPL2; NbExp=3; IntAct=EBI-12056025, EBI-17566767;
CC Q14162; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12056025, EBI-16439278;
CC Q14162; Q9HC36: MRM3; NbExp=3; IntAct=EBI-12056025, EBI-1045440;
CC Q14162; O14524-2: NEMP1; NbExp=3; IntAct=EBI-12056025, EBI-10969203;
CC Q14162; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-12056025, EBI-5235586;
CC Q14162; P22735: TGM1; NbExp=3; IntAct=EBI-12056025, EBI-2562368;
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 Name=5; Synonyms=SREC-2;
CC IsoId=Q14162-5; Sequence=VSP_039958, VSP_039959;
CC -!- TISSUE SPECIFICITY: Endothelial cells.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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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 AlphaFoldDB; Q14162; -.
DR SMR; Q14162; -.
DR BioGRID; 114146; 20.
DR IntAct; Q14162; 21.
DR MINT; Q14162; -.
DR STRING; 9606.ENSP00000263071; -.
DR GlyGen; Q14162; 3 sites.
DR iPTMnet; Q14162; -.
DR PhosphoSitePlus; Q14162; -.
DR SwissPalm; Q14162; -.
DR BioMuta; SCARF1; -.
DR DMDM; 311033530; -.
DR jPOST; Q14162; -.
DR MassIVE; Q14162; -.
DR PaxDb; Q14162; -.
DR PeptideAtlas; Q14162; -.
DR PRIDE; Q14162; -.
DR ProteomicsDB; 59887; -. [Q14162-1]
DR ProteomicsDB; 59888; -. [Q14162-2]
DR ProteomicsDB; 59889; -. [Q14162-3]
DR ProteomicsDB; 59890; -. [Q14162-4]
DR ProteomicsDB; 59891; -. [Q14162-5]
DR Antibodypedia; 22736; 151 antibodies from 35 providers.
DR DNASU; 8578; -.
DR Ensembl; ENST00000263071.9; ENSP00000263071.4; ENSG00000074660.17. [Q14162-1]
DR Ensembl; ENST00000434376.6; ENSP00000411167.2; ENSG00000074660.17. [Q14162-5]
DR Ensembl; ENST00000571272.5; ENSP00000458174.1; ENSG00000074660.17. [Q14162-3]
DR Ensembl; ENST00000621348.4; ENSP00000481595.1; ENSG00000276336.4. [Q14162-1]
DR Ensembl; ENST00000631462.1; ENSP00000487665.1; ENSG00000276336.4. [Q14162-5]
DR Ensembl; ENST00000632317.1; ENSP00000488776.1; ENSG00000276336.4. [Q14162-3]
DR GeneID; 8578; -.
DR KEGG; hsa:8578; -.
DR MANE-Select; ENST00000263071.9; ENSP00000263071.4; NM_003693.4; NP_003684.2.
DR UCSC; uc002fsy.3; human. [Q14162-1]
DR CTD; 8578; -.
DR DisGeNET; 8578; -.
DR GeneCards; SCARF1; -.
DR HGNC; HGNC:16820; SCARF1.
DR HPA; ENSG00000074660; Tissue enhanced (lymphoid).
DR MIM; 607873; gene.
DR neXtProt; NX_Q14162; -.
DR OpenTargets; ENSG00000074660; -.
DR PharmGKB; PA38420; -.
DR VEuPathDB; HostDB:ENSG00000074660; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00950000183101; -.
DR HOGENOM; CLU_017821_0_0_1; -.
DR InParanoid; Q14162; -.
DR OMA; CFHGNCH; -.
DR PhylomeDB; Q14162; -.
DR TreeFam; TF332598; -.
DR PathwayCommons; Q14162; -.
DR Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
DR SignaLink; Q14162; -.
DR BioGRID-ORCS; 8578; 73 hits in 1074 CRISPR screens.
DR GenomeRNAi; 8578; -.
DR Pharos; Q14162; Tbio.
DR PRO; PR:Q14162; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14162; protein.
DR Bgee; ENSG00000074660; Expressed in spleen and 94 other tissues.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR033329; SCARF1.
DR InterPro; IPR042635; SREC1/2.
DR PANTHER; PTHR24043; PTHR24043; 1.
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; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..830
FT /note="Scavenger receptor class F member 1"
FT /id="PRO_0000007738"
FT TOPO_DOM 20..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 53..87
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 95..130
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 155..191
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 215..249
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 302..339
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 351..382
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 516..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5ND28"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 63..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 99..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 105..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 120..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 159..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 165..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 181..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 219..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 225..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 239..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 306..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 313..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 355..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 358..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 372..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 330..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11978792"
FT /id="VSP_039956"
FT VAR_SEQ 338..830
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11978792"
FT /id="VSP_039957"
FT VAR_SEQ 338..342
FT /note="CEDPC -> GPVIL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11978792"
FT /id="VSP_039958"
FT VAR_SEQ 343..830
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11978792"
FT /id="VSP_039959"
FT VAR_SEQ 496..569
FT /note="VSHHDPEVPFNHSFIEPPSAGWATDDSFSSDPESGEADEVPAYCVPPQEGMV
FT PVAQAGSSEASLAAGAFPPPED -> ASSSRPLPAGPLMTPSHPILSLERQMRFLPTVC
FT HPKKGWSLWPRQGRQRPAWLQVLSRPLRTPPRHSPSRAPPA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11978792"
FT /id="VSP_039960"
FT VAR_SEQ 570..830
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11978792"
FT /id="VSP_039961"
FT VARIANT 425
FT /note="A -> V (in dbSNP:rs2272011)"
FT /evidence="ECO:0000269|PubMed:11978792,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8590280,
FT ECO:0000269|PubMed:9395444, ECO:0000269|Ref.5"
FT /id="VAR_047249"
FT VARIANT 618
FT /note="R -> K (in dbSNP:rs35455643)"
FT /id="VAR_047250"
FT VARIANT 639
FT /note="E -> D (in dbSNP:rs3744644)"
FT /evidence="ECO:0000269|PubMed:11978792,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8590280,
FT ECO:0000269|PubMed:9395444"
FT /id="VAR_047251"
FT VARIANT 662
FT /note="R -> W (in dbSNP:rs8072430)"
FT /evidence="ECO:0000269|PubMed:8590280,
FT ECO:0000269|PubMed:9395444"
FT /id="VAR_047252"
FT VARIANT 667
FT /note="G -> S (in dbSNP:rs4790250)"
FT /evidence="ECO:0000269|PubMed:11978792,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8590280,
FT ECO:0000269|PubMed:9395444"
FT /id="VAR_047253"
FT VARIANT 748
FT /note="G -> V (in dbSNP:rs3760460)"
FT /id="VAR_047254"
FT CONFLICT 328..329
FT /note="RC -> PG (in Ref. 2; BAC02696)"
FT /evidence="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
