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C4BPA_HUMAN
ID   C4BPA_HUMAN             Reviewed;         597 AA.
AC   P04003; Q5VVQ8;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   03-AUG-2022, entry version 204.
DE   RecName: Full=C4b-binding protein alpha chain;
DE            Short=C4bp;
DE   AltName: Full=Proline-rich protein;
DE            Short=PRP;
DE   Flags: Precursor;
GN   Name=C4BPA; Synonyms=C4BP;
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].
RC   TISSUE=Liver;
RX   PubMed=2590215; DOI=10.1016/0006-291x(89)91045-0;
RA   Matsuguchi T., Okamura S., Aso T., Sata T., Niho Y.;
RT   "Molecular cloning of the cDNA coding for proline-rich protein (PRP):
RT   identity of PRP as C4b-binding protein.";
RL   Biochem. Biophys. Res. Commun. 165:138-144(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1989602; DOI=10.1016/0006-291x(91)90509-6;
RA   Aso T., Okamura S., Matsuguchi T., Sakamoto N., Sata T., Niho Y.;
RT   "Genomic organization of the alpha chain of the human C4b-binding protein
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 174:222-227(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 9-81.
RX   PubMed=3378624; DOI=10.1016/0014-5793(88)80763-4;
RA   Lintin S.J., Lewin A.R., Reid K.B.M.;
RT   "Derivation of the sequence of the signal peptide in human C4b-binding
RT   protein and interspecies cross-hybridisation of the C4bp cDNA sequence.";
RL   FEBS Lett. 232:328-332(1988).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-288.
RX   PubMed=3017751; DOI=10.1016/0014-5793(86)81390-4;
RA   Lintin S.J., Reid K.B.M.;
RT   "Studies on the structure of the human C4b-binding protein gene.";
RL   FEBS Lett. 204:77-81(1986).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 80-597.
RX   PubMed=3840370; DOI=10.1042/bj2300133;
RA   Chung L.P., Bentley D.R., Reid K.B.M.;
RT   "Molecular cloning and characterization of the cDNA coding for C4b-binding
RT   protein, a regulatory protein of the classical pathway of the human
RT   complement system.";
RL   Biochem. J. 230:133-141(1985).
RN   [9]
RP   PROTEIN SEQUENCE OF 49-88.
RX   PubMed=4033666; DOI=10.1016/0161-5890(85)90127-0;
RA   Chung L.P., Gagnon J., Reid K.B.M.;
RT   "Amino acid sequence studies of human C4b-binding protein: N-terminal
RT   sequence analysis and alignment of the fragments produced by limited
RT   proteolysis with chymotrypsin and the peptides produced by cyanogen bromide
RT   treatment.";
RL   Mol. Immunol. 22:427-435(1985).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-506 AND ASN-528.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-506.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-506.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [13]
RP   IDENTIFICATION 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., 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).
RN   [14]
RP   INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SDRE (MICROBIAL INFECTION).
RX   PubMed=24600566; DOI=10.1016/j.rinim.2013.10.004;
RA   Hair P.S., Foley C.K., Krishna N.K., Nyalwidhe J.O., Geoghegan J.A.,
RA   Foster T.J., Cunnion K.M.;
RT   "Complement regulator C4BP binds to Staphylococcus aureus surface proteins
RT   SdrE and Bbp inhibiting bacterial opsonization and killing.";
RL   Results Immunol. 3:114-121(2013).
RN   [15]
RP   STRUCTURE BY ELECTRON MICROSCOPY, AND LIGAND-BINDING.
RX   PubMed=6222381; DOI=10.1073/pnas.80.11.3461;
RA   Dahlback B., Smith C.A., Mueller-Eberhard H.J.;
RT   "Visualization of human C4b-binding protein and its complexes with vitamin
RT   K-dependent protein S and complement protein C4b.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:3461-3465(1983).
RN   [16]
RP   STRUCTURE BY NMR OF 49-172, AND DISULFIDE BONDS.
RX   PubMed=16330538; DOI=10.1074/jbc.m511563200;
RA   Jenkins H.T., Mark L., Ball G., Persson J., Lindahl G., Uhrin D.,
RA   Blom A.M., Barlow P.N.;
RT   "Human C4b-binding protein, structural basis for interaction with
RT   streptococcal M protein, a major bacterial virulence factor.";
RL   J. Biol. Chem. 281:3690-3697(2006).
CC   -!- FUNCTION: Controls the classical pathway of complement activation. It
CC       binds as a cofactor to C3b/C4b inactivator (C3bINA), which then
CC       hydrolyzes the complement fragment C4b. It also accelerates the
CC       degradation of the C4bC2a complex (C3 convertase) by dissociating the
CC       complement fragment C2a. Alpha chain binds C4b. It interacts also with
CC       anticoagulant protein S and with serum amyloid P component.
CC   -!- SUBUNIT: Disulfide-linked complex of alpha and beta chains of 3
CC       possible sorts: a 570 kDa complex of 7 alpha chains and 1 beta chain, a
CC       530 kDa homoheptamer of alpha chains or a 500 kDa complex of 6 alpha
CC       chains and 1 beta chain. The central body of the alpha chain homomer
CC       supports tentacles, each with the binding site for C4b at the end.
CC       {ECO:0000269|PubMed:16330538}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC       protein SdrE; this interaction inhibits complement-mediated bacterial
CC       opsonization. {ECO:0000269|PubMed:24600566}.
CC   -!- INTERACTION:
CC       P04003; PRO_0000023526 [P02741]: CRP; NbExp=4; IntAct=EBI-978348, EBI-22033103;
CC       P04003; P13050: arp4; Xeno; NbExp=5; IntAct=EBI-978348, EBI-978341;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Chylomicrons in the plasma.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; M31452; AAA36507.1; -; mRNA.
DR   EMBL; M62486; AAA36506.1; -; Genomic_DNA.
DR   EMBL; M62475; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62476; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62477; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62478; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62479; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62480; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62481; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62482; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62484; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; M62485; AAA36506.1; JOINED; Genomic_DNA.
DR   EMBL; AK313164; BAG35982.1; -; mRNA.
DR   EMBL; CH471100; EAW93502.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93503.1; -; Genomic_DNA.
DR   EMBL; BC022312; AAH22312.1; -; mRNA.
DR   EMBL; X07853; CAA30701.1; -; mRNA.
DR   EMBL; X04284; CAB51244.1; -; Genomic_DNA.
DR   EMBL; X04296; CAA27839.1; -; Genomic_DNA.
DR   EMBL; X02865; CAA26617.1; -; mRNA.
DR   CCDS; CCDS1477.1; -.
DR   PIR; A33568; NBHUC4.
DR   RefSeq; NP_000706.1; NM_000715.3.
DR   RefSeq; XP_005273308.1; XM_005273251.1.
DR   RefSeq; XP_005273309.1; XM_005273252.4.
DR   PDB; 2A55; NMR; -; A=49-172.
DR   PDB; 4B0F; X-ray; 2.80 A; A/B/C/D/E/F/G=540-597.
DR   PDB; 5HYP; X-ray; 3.02 A; A=49-172.
DR   PDB; 5HYT; X-ray; 2.54 A; B/D/F/H=49-172.
DR   PDB; 5HYU; X-ray; 2.56 A; B=49-172.
DR   PDB; 5HZP; X-ray; 2.74 A; B/D=49-172.
DR   PDB; 5I0Q; X-ray; 2.29 A; B=49-172.
DR   PDBsum; 2A55; -.
DR   PDBsum; 4B0F; -.
DR   PDBsum; 5HYP; -.
DR   PDBsum; 5HYT; -.
DR   PDBsum; 5HYU; -.
DR   PDBsum; 5HZP; -.
DR   PDBsum; 5I0Q; -.
DR   AlphaFoldDB; P04003; -.
DR   SMR; P04003; -.
DR   BioGRID; 107183; 42.
DR   IntAct; P04003; 26.
DR   STRING; 9606.ENSP00000356037; -.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   CarbonylDB; P04003; -.
DR   GlyConnect; 1051; 9 N-Linked glycans (2 sites).
DR   GlyGen; P04003; 9 sites, 19 N-linked glycans (2 sites), 2 O-linked glycans (5 sites).
DR   iPTMnet; P04003; -.
DR   PhosphoSitePlus; P04003; -.
DR   BioMuta; C4BPA; -.
DR   DMDM; 416733; -.
DR   jPOST; P04003; -.
DR   MassIVE; P04003; -.
DR   PaxDb; P04003; -.
DR   PeptideAtlas; P04003; -.
DR   PRIDE; P04003; -.
DR   ProteomicsDB; 51632; -.
DR   Antibodypedia; 694; 300 antibodies from 29 providers.
DR   DNASU; 722; -.
DR   Ensembl; ENST00000367070.8; ENSP00000356037.3; ENSG00000123838.11.
DR   GeneID; 722; -.
DR   KEGG; hsa:722; -.
DR   MANE-Select; ENST00000367070.8; ENSP00000356037.3; NM_000715.4; NP_000706.1.
DR   UCSC; uc001hfo.3; human.
DR   CTD; 722; -.
DR   DisGeNET; 722; -.
DR   GeneCards; C4BPA; -.
DR   HGNC; HGNC:1325; C4BPA.
DR   HPA; ENSG00000123838; Tissue enriched (liver).
DR   MIM; 120830; gene.
DR   neXtProt; NX_P04003; -.
DR   OpenTargets; ENSG00000123838; -.
DR   PharmGKB; PA25905; -.
DR   VEuPathDB; HostDB:ENSG00000123838; -.
DR   eggNOG; ENOG502SHRK; Eukaryota.
DR   GeneTree; ENSGT00940000154640; -.
DR   HOGENOM; CLU_020107_5_2_1; -.
DR   InParanoid; P04003; -.
DR   OMA; WKPQIPS; -.
DR   OrthoDB; 1058295at2759; -.
DR   PhylomeDB; P04003; -.
DR   TreeFam; TF334137; -.
DR   PathwayCommons; P04003; -.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SignaLink; P04003; -.
DR   BioGRID-ORCS; 722; 9 hits in 1066 CRISPR screens.
DR   ChiTaRS; C4BPA; human.
DR   EvolutionaryTrace; P04003; -.
DR   GenomeRNAi; 722; -.
DR   Pharos; P04003; Tbio.
DR   PRO; PR:P04003; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P04003; protein.
DR   Bgee; ENSG00000123838; Expressed in right lobe of liver and 114 other tissues.
DR   ExpressionAtlas; P04003; baseline and differential.
DR   Genevisible; P04003; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IDA:BHF-UCL.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
DR   GO; GO:1903027; P:regulation of opsonization; IDA:BHF-UCL.
DR   GO; GO:0009609; P:response to symbiotic bacterium; IDA:BHF-UCL.
DR   CDD; cd00033; CCP; 8.
DR   InterPro; IPR040514; C4bp_oligo.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF18453; C4bp_oligo; 1.
DR   Pfam; PF00084; Sushi; 8.
DR   SMART; SM00032; CCP; 8.
DR   SUPFAM; SSF57535; SSF57535; 8.
DR   PROSITE; PS50923; SUSHI; 8.
PE   1: Evidence at protein level;
KW   3D-structure; Complement pathway; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW   Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL          1..48
FT                   /evidence="ECO:0000269|PubMed:4033666"
FT   CHAIN           49..597
FT                   /note="C4b-binding protein alpha chain"
FT                   /id="PRO_0000005888"
FT   DOMAIN          49..110
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          111..172
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          173..236
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          237..296
FT                   /note="Sushi 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          297..362
FT                   /note="Sushi 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          363..424
FT                   /note="Sushi 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          425..482
FT                   /note="Sushi 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          483..540
FT                   /note="Sushi 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3840370"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:3840370"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:3840370"
FT   DISULFID        50..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT                   ECO:0000269|PubMed:16330538"
FT   DISULFID        81..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT                   ECO:0000269|PubMed:16330538"
FT   DISULFID        113..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT                   ECO:0000269|PubMed:16330538"
FT   DISULFID        140..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT                   ECO:0000269|PubMed:16330538"
FT   DISULFID        175..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        203..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        239..281
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        267..294
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        299..348
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        332..360
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        365..409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        399..422
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        426..468
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        454..480
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        484..525
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        511..538
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        546
FT                   /note="Interchain (with beta chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        558
FT                   /note="Interchain (with beta chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   VARIANT         4
FT                   /note="P -> Q (in dbSNP:rs55867570)"
FT                   /id="VAR_061123"
FT   VARIANT         60
FT                   /note="A -> V (in dbSNP:rs17020956)"
FT                   /id="VAR_048815"
FT   VARIANT         240
FT                   /note="R -> H (in dbSNP:rs45574833)"
FT                   /id="VAR_061124"
FT   VARIANT         300
FT                   /note="I -> T (in dbSNP:rs4844573)"
FT                   /id="VAR_024420"
FT   VARIANT         357
FT                   /note="Y -> H"
FT                   /id="VAR_001978"
FT   VARIANT         473
FT                   /note="W -> L (in dbSNP:rs1801341)"
FT                   /id="VAR_012038"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:5HYP"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:5HYP"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          122..128
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:5HZP"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          150..157
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:5I0Q"
FT   HELIX           547..555
FT                   /evidence="ECO:0007829|PDB:4B0F"
FT   STRAND          558..561
FT                   /evidence="ECO:0007829|PDB:4B0F"
FT   HELIX           562..589
FT                   /evidence="ECO:0007829|PDB:4B0F"
FT   HELIX           591..596
FT                   /evidence="ECO:0007829|PDB:4B0F"
SQ   SEQUENCE   597 AA;  67033 MW;  67E03F2EA85A16DD CRC64;
     MHPPKTPSGA LHRKRKMAAW PFSRLWKVSD PILFQMTLIA ALLPAVLGNC GPPPTLSFAA
     PMDITLTETR FKTGTTLKYT CLPGYVRSHS TQTLTCNSDG EWVYNTFCIY KRCRHPGELR
     NGQVEIKTDL SFGSQIEFSC SEGFFLIGST TSRCEVQDRG VGWSHPLPQC EIVKCKPPPD
     IRNGRHSGEE NFYAYGFSVT YSCDPRFSLL GHASISCTVE NETIGVWRPS PPTCEKITCR
     KPDVSHGEMV SGFGPIYNYK DTIVFKCQKG FVLRGSSVIH CDADSKWNPS PPACEPNSCI
     NLPDIPHASW ETYPRPTKED VYVVGTVLRY RCHPGYKPTT DEPTTVICQK NLRWTPYQGC
     EALCCPEPKL NNGEITQHRK SRPANHCVYF YGDEISFSCH ETSRFSAICQ GDGTWSPRTP
     SCGDICNFPP KIAHGHYKQS SSYSFFKEEI IYECDKGYIL VGQAKLSCSY SHWSAPAPQC
     KALCRKPELV NGRLSVDKDQ YVEPENVTIQ CDSGYGVVGP QSITCSGNRT WYPEVPKCEW
     ETPEGCEQVL TGKRLMQCLP NPEDVKMALE VYKLSLEIEQ LELQRDSARQ STLDKEL
 
 
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