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C-reactive protein [Cleaved into: C-reactive protein(1-205)]

 CRP_HUMAN               Reviewed;         224 AA.
P02741; A8K078; D3DVD9; D3DVE0; Q08AK3; Q8WW75;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
18-JUL-2018, entry version 214.
RecName: Full=C-reactive protein;
Contains:
RecName: Full=C-reactive protein(1-205);
Flags: Precursor;
Name=CRP; Synonyms=PTX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2997165;
Lei K.-J., Liu T., Zon G., Soravia E., Liu T.-Y., Goldman N.D.;
"Genomic DNA sequence for human C-reactive protein.";
J. Biol. Chem. 260:13377-13383(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3840479;
Woo P., Korenberg J.R., Whitehead A.S.;
"Characterization of genomic and complementary DNA sequence of human
C-reactive protein, and comparison with the complementary DNA sequence
of serum amyloid P component.";
J. Biol. Chem. 260:13384-13388(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Murphy T.M., Baum L., Beaman K.;
"Extrahepetic transcription of human C-reactive protein.";
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Tenchini M.L., Marchetti L., Bossi E., Malcovati M., Lorenzetti R.;
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Harraghy N.;
"Controlled gene expression using acute phase response elements.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-26.
PubMed=6685157;
Tucci A., Goldberger G., Whitehead A.S., Kay R.M., Woods D.E.,
Colten H.R.;
"Biosynthesis and postsynthetic processing of human C-reactive
protein.";
J. Immunol. 131:2416-2419(1983).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 144-175.
PubMed=6857266; DOI=10.1126/science.6857266;
Whitehead A.S., Bruns G.A.P., Markham A.F., Colten H.R., Woods D.E.;
"Isolation of human C-reactive protein complementary DNA and
localization of the gene to chromosome 1.";
Science 221:69-71(1983).
[13]
PROTEIN SEQUENCE OF 19-224, AND PYROGLUTAMATE FORMATION AT GLN-19.
PubMed=762075;
Oliveira E.B., Gotschlich E.C., Liu T.-Y.;
"Primary structure of human C-reactive protein.";
J. Biol. Chem. 254:489-502(1979).
[14]
PROTEIN SEQUENCE OF 22-55.
PubMed=403526; DOI=10.1073/pnas.74.3.1214;
Osmand A.P., Gewurz H., Friedenson B.;
"Partial amino-acid sequences of human and rabbit C-reactive proteins:
homology with immunoglobulins and histocompatibility antigens.";
Proc. Natl. Acad. Sci. U.S.A. 74:1214-1218(1977).
[15]
MASS SPECTROMETRY.
Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.;
"Selected expression profiling of full-length proteins and their
variants in human plasma.";
Clin. Proteomics 1:7-16(2004).
[16]
INTERACTION WITH FCN1.
PubMed=21037097; DOI=10.4049/jimmunol.1001225;
Zhang J., Yang L., Ang Z., Yoong S.L., Tran T.T., Anand G.S.,
Tan N.S., Ho B., Ding J.L.;
"Secreted M-ficolin anchors onto monocyte transmembrane G protein-
coupled receptor 43 and cross talks with plasma C-reactive protein to
mediate immune signaling and regulate host defense.";
J. Immunol. 185:6899-6910(2010).
[17]
3D-STRUCTURE MODELING.
PubMed=7881902; DOI=10.1016/S0969-2126(94)00105-7;
Srinivasan N., White H.E., Emsley J., Wood S.P., Pepys M.B.,
Blundell T.L.;
"Comparative analyses of pentraxins: implications for protomer
assembly and ligand binding.";
Structure 2:1017-1027(1994).
[18]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=8599761; DOI=10.1038/nsb0496-346;
Shrive A.K., Cheetham G.M.T., Holden D., Myles D.A.A., Turnell W.G.,
Volanakis J.E., Pepys M.B., Bloomer A.C., Greenhough T.J.;
"Three dimensional structure of human C-reactive protein.";
Nat. Struct. Biol. 3:346-353(1996).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=10368284; DOI=10.1016/S0969-2126(99)80023-9;
Thompson D., Pepys M.B., Wood S.P.;
"The physiological structure of human C-reactive protein and its
complex with phosphocholine.";
Structure 7:169-177(1999).
-!- FUNCTION: Displays several functions associated with host defense:
it promotes agglutination, bacterial capsular swelling,
phagocytosis and complement fixation through its calcium-dependent
binding to phosphorylcholine. Can interact with DNA and histones
and may scavenge nuclear material released from damaged
circulating cells.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- SUBUNIT: Homopentamer. Pentraxin (or pentaxin) have a discoid
arrangement of 5 non-covalently bound subunits. Interacts with
FCN1; may regulate monocyte activation by FCN1.
{ECO:0000269|PubMed:21037097}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1395983, EBI-1395983;
P31995:FCGR2C; NbExp=2; IntAct=EBI-1395983, EBI-1396036;
Q96IJ6:GMPPA; NbExp=3; IntAct=EBI-1395983, EBI-750953;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P02741-1; Sequence=Displayed;
Name=2;
IsoId=P02741-2; Sequence=VSP_004656;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Found in plasma.
-!- INDUCTION: The concentration of CRP in plasma increases greatly
during acute phase response to tissue injury, infection or other
inflammatory stimuli. It is induced by IL1/interleukin-1 and
IL6/interleukin-6.
-!- MASS SPECTROMETRY: Mass=23028; Method=MALDI; Range=19-224;
Evidence={ECO:0000269|Ref.15};
-!- MASS SPECTROMETRY: Mass=22930; Method=MALDI; Range=19-223;
Evidence={ECO:0000269|Ref.15};
-!- MISCELLANEOUS: This protein owes its name to its ability
precipitate pneumococcal C-polysaccharide in the presence of
calcium.
-!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=C-reactive protein entry;
URL="https://en.wikipedia.org/wiki/C-reactive_protein";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/crp/";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=No more Christmas
pudding? - Issue 30 of January 2003;
URL="https://web.expasy.org/spotlight/back_issues/030";
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EMBL; M11880; AAB59526.1; -; Genomic_DNA.
EMBL; M11725; AAA52075.1; -; Genomic_DNA.
EMBL; X56692; CAA40020.1; -; mRNA.
EMBL; X56214; CAA39671.1; -; mRNA.
EMBL; AF442818; AAL48218.2; -; Genomic_DNA.
EMBL; AK289443; BAF82132.1; -; mRNA.
EMBL; AF449713; AAL40835.1; -; Genomic_DNA.
EMBL; AL445528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52778.1; -; Genomic_DNA.
EMBL; CH471121; EAW52779.1; -; Genomic_DNA.
EMBL; CH471121; EAW52780.1; -; Genomic_DNA.
EMBL; BC020766; AAH20766.1; -; mRNA.
EMBL; BC125135; AAI25136.1; -; mRNA.
EMBL; M35163; AAA52076.1; -; mRNA.
EMBL; K00518; AAA52074.1; -; mRNA.
CCDS; CCDS30911.1; -. [P02741-1]
PIR; A24515; CJHU.
RefSeq; NP_000558.2; NM_000567.2. [P02741-1]
RefSeq; NP_001315986.1; NM_001329057.1. [P02741-1]
RefSeq; NP_001315987.1; NM_001329058.1. [P02741-2]
UniGene; Hs.709456; -.
UniGene; Hs.76452; -.
PDB; 1B09; X-ray; 2.50 A; A/B/C/D/E=19-224.
PDB; 1CRV; Model; -; A/B/C/D/E=19-224.
PDB; 1GNH; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=19-224.
PDB; 1LJ7; X-ray; 3.15 A; A/B/C/D/E/F/G/H/I/J=19-224.
PDB; 3L2Y; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=19-224.
PDB; 3PVN; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=19-224.
PDB; 3PVO; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=19-224.
PDBsum; 1B09; -.
PDBsum; 1CRV; -.
PDBsum; 1GNH; -.
PDBsum; 1LJ7; -.
PDBsum; 3L2Y; -.
PDBsum; 3PVN; -.
PDBsum; 3PVO; -.
ProteinModelPortal; P02741; -.
SMR; P02741; -.
BioGrid; 107791; 50.
DIP; DIP-39125N; -.
IntAct; P02741; 12.
MINT; P02741; -.
STRING; 9606.ENSP00000255030; -.
DrugBank; DB05744; CRx-139.
UniLectin; P02741; -.
iPTMnet; P02741; -.
PhosphoSitePlus; P02741; -.
BioMuta; CRP; -.
DMDM; 117486; -.
DOSAC-COBS-2DPAGE; P02741; -.
SWISS-2DPAGE; P02741; -.
PaxDb; P02741; -.
PeptideAtlas; P02741; -.
PRIDE; P02741; -.
ProteomicsDB; 12625; -. [P02741-2]
ProteomicsDB; 51558; -.
ProteomicsDB; 51559; -. [P02741-2]
Ensembl; ENST00000255030; ENSP00000255030; ENSG00000132693. [P02741-1]
Ensembl; ENST00000368112; ENSP00000357093; ENSG00000132693. [P02741-2]
GeneID; 1401; -.
KEGG; hsa:1401; -.
UCSC; uc001ftw.3; human. [P02741-1]
CTD; 1401; -.
DisGeNET; 1401; -.
EuPathDB; HostDB:ENSG00000132693.12; -.
GeneCards; CRP; -.
H-InvDB; HIX0028720; -.
HGNC; HGNC:2367; CRP.
HPA; CAB005036; -.
HPA; HPA027367; -.
HPA; HPA027396; -.
MIM; 123260; gene.
neXtProt; NX_P02741; -.
OpenTargets; ENSG00000132693; -.
PharmGKB; PA120; -.
eggNOG; ENOG410J9V0; Eukaryota.
eggNOG; ENOG410YIJN; LUCA.
GeneTree; ENSGT00760000119128; -.
HOGENOM; HOG000247043; -.
HOVERGEN; HBG005405; -.
InParanoid; P02741; -.
KO; K16143; -.
OMA; NEILIFW; -.
OrthoDB; EOG091G0H6X; -.
PhylomeDB; P02741; -.
TreeFam; TF330208; -.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
SIGNOR; P02741; -.
ChiTaRS; CRP; human.
EvolutionaryTrace; P02741; -.
GeneWiki; C-reactive_protein; -.
GenomeRNAi; 1401; -.
PRO; PR:P02741; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000132693; -.
CleanEx; HS_CRP; -.
ExpressionAtlas; P02741; baseline and differential.
Genevisible; P02741; HS.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0033265; F:choline binding; TAS:BHF-UCL.
GO; GO:0001849; F:complement component C1q binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:AgBase.
GO; GO:0006953; P:acute-phase response; TAS:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; TAS:BHF-UCL.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0097756; P:negative regulation of blood vessel diameter; IDA:AgBase.
GO; GO:0010888; P:negative regulation of lipid storage; IDA:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
GO; GO:0008228; P:opsonization; TAS:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:AgBase.
GO; GO:2000482; P:regulation of interleukin-8 secretion; IDA:UniProtKB.
CDD; cd00152; PTX; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR030476; Pentaxin_CS.
InterPro; IPR001759; Pentraxin-related.
Pfam; PF00354; Pentaxin; 1.
PRINTS; PR00895; PENTAXIN.
SMART; SM00159; PTX; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00289; PTX_1; 1.
PROSITE; PS51828; PTX_2; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Alternative splicing; Calcium;
Complete proteome; Direct protein sequencing; Disulfide bond;
Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:762075}.
CHAIN 19 224 C-reactive protein.
/FTId=PRO_0000023526.
CHAIN 19 223 C-reactive protein(1-205).
/FTId=PRO_0000023527.
DOMAIN 23 224 Pentraxin (PTX). {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 78 78 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 79 79 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 156 156 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 156 156 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 157 157 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU01172}.
METAL 158 158 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 158 158 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 168 168 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
MOD_RES 19 19 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:762075}.
DISULFID 54 115 {ECO:0000255|PROSITE-ProRule:PRU01172,
ECO:0000269|PubMed:762075}.
VAR_SEQ 67 199 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004656.
CONFLICT 49 49 K -> G (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 52 52 T -> G (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 67 82 YSIFSYATKRQDNEIL -> TVFSRMPPRDKTMRFF (in
Ref. 4; CAA39671). {ECO:0000305}.
CONFLICT 80 98 Missing (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 170 170 L -> V (in Ref. 12; AAA52074).
{ECO:0000305}.
STRAND 25 29 {ECO:0000244|PDB:3PVN}.
STRAND 37 40 {ECO:0000244|PDB:3PVN}.
STRAND 48 60 {ECO:0000244|PDB:3PVN}.
HELIX 61 63 {ECO:0000244|PDB:3PVN}.
STRAND 67 74 {ECO:0000244|PDB:3PVN}.
STRAND 77 86 {ECO:0000244|PDB:3PVN}.
TURN 87 89 {ECO:0000244|PDB:3PVN}.
STRAND 90 95 {ECO:0000244|PDB:3PVN}.
STRAND 98 103 {ECO:0000244|PDB:3PVN}.
STRAND 112 119 {ECO:0000244|PDB:3PVN}.
TURN 120 122 {ECO:0000244|PDB:3PVN}.
STRAND 124 129 {ECO:0000244|PDB:3PVN}.
STRAND 132 138 {ECO:0000244|PDB:1LJ7}.
STRAND 150 155 {ECO:0000244|PDB:3PVN}.
HELIX 166 168 {ECO:0000244|PDB:3PVN}.
STRAND 172 182 {ECO:0000244|PDB:3PVN}.
HELIX 186 194 {ECO:0000244|PDB:3PVN}.
STRAND 201 203 {ECO:0000244|PDB:3PVN}.
HELIX 205 207 {ECO:0000244|PDB:1B09}.
STRAND 210 215 {ECO:0000244|PDB:3PVN}.
STRAND 217 220 {ECO:0000244|PDB:3PVN}.
SEQUENCE 224 AA; 25039 MW; 669228636A8544F6 CRC64;
MEKLLCFLVL TSLSHAFGQT DMSRKAFVFP KESDTSYVSL KAPLTKPLKA FTVCLHFYTE
LSSTRGYSIF SYATKRQDNE ILIFWSKDIG YSFTVGGSEI LFEVPEVTVA PVHICTSWES
ASGIVEFWVD GKPRVRKSLK KGYTVGAEAS IILGQEQDSF GGNFEGSQSL VGDIGNVNMW
DFVLSPDEIN TIYLGGPFSP NVLNWRALKY EVQGEVFTKP QLWP


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