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Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; C3-beta-c (C3bc); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]

 CO3_BOVIN               Reviewed;        1661 AA.
Q2UVX4; Q2KIZ4;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 89.
RecName: Full=Complement C3;
Contains:
RecName: Full=Complement C3 beta chain;
Contains:
RecName: Full=Complement C3 alpha chain;
Contains:
RecName: Full=C3a anaphylatoxin;
Contains:
RecName: Full=C3-beta-c;
Short=C3bc;
Contains:
RecName: Full=Acylation stimulating protein;
Short=ASP;
AltName: Full=C3adesArg;
Contains:
RecName: Full=Complement C3b alpha' chain;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 1;
Contains:
RecName: Full=Complement C3dg fragment;
Contains:
RecName: Full=Complement C3g fragment;
Contains:
RecName: Full=Complement C3d fragment;
Contains:
RecName: Full=Complement C3f fragment;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 2;
Flags: Precursor;
Name=C3;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (3.0
ANGSTROMS) OF C3.
PubMed=16831446; DOI=10.1016/j.jmb.2006.06.009;
Fredslund F., Jenner L., Husted L.B., Nyborg J., Andersen G.R.,
Sottrup-Jensen L.;
"The structure of bovine complement component 3 reveals the basis for
thioester function.";
J. Mol. Biol. 361:115-127(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH BHV-1 GLYCOPROTEIN C.
PubMed=8390825; DOI=10.1007/BF01309666;
Huemer H.P., Larcher C., van Drunen Littel-van den Hurk S.,
Babiuk L.A.;
"Species selective interaction of Alphaherpesvirinae with the
'unspecific' immune system of the host.";
Arch. Virol. 130:353-364(1993).
-!- FUNCTION: C3 plays a central role in the activation of the
complement system. Its processing by C3 convertase is the central
reaction in both classical and alternative complement pathways.
After activation C3b can bind covalently, via its reactive
thioester, to cell surface carbohydrates or immune aggregates (By
similarity). {ECO:0000250}.
-!- FUNCTION: Derived from proteolytic degradation of complement C3,
C3a anaphylatoxin is a mediator of local inflammatory process. It
induces the contraction of smooth muscle, increases vascular
permeability and causes histamine release from mast cells and
basophilic leukocytes. In chronic inflammation, acts as a
chemoattractant for neutrophils (By similarity). {ECO:0000250}.
-!- FUNCTION: C3-beta-c: Acts as a chemoattractant for neutrophils in
chronic inflammation. {ECO:0000250}.
-!- FUNCTION: Acylation stimulating protein: adipogenic hormone that
stimulates triglyceride (TG) synthesis and glucose transport in
adipocytes, regulating fat storage and playing a role in
postprandial TG clearance. Appears to stimulate TG synthesis via
activation of the PLC, MAPK and AKT signaling pathways. Ligand for
C5AR2. Promotes the phosphorylation, ARRB2-internalization and
recycling of C5AR2 (By similarity). {ECO:0000250}.
-!- SUBUNIT: C3 precursor is first processed by the removal of 4 Arg
residues, forming two chains, beta and alpha, linked by a
disulfide bond. C3 convertase activates C3 by cleaving the alpha
chain, releasing C3a anaphylatoxin and generating C3b (beta chain
+ alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi
domains 1 and 2). Interacts with VSIG4. Interacts (both C3a and
ASP) with C5AR2; the interaction occurs with higher affinity for
ASP, enhancing the phosphorylation and activation of C5AR2,
recruitment of ARRB2 to the cell surface and endocytosis of GRP77
(By similarity). Interacts with BHV-1 glycoprotein C.
{ECO:0000250, ECO:0000269|PubMed:8390825}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: C3b is rapidly split in two positions by factor I and a
cofactor to form iC3b (inactivated C3b) and C3f which is released.
Then iC3b is slowly cleaved (possibly by factor I) to form C3c
(beta chain + alpha' chain fragment 1 + alpha' chain fragment 2),
C3dg and C3f. Other proteases produce other fragments such as C3d
or C3g. C3a is further processed by carboxypeptidases to release
the C-terminal arginine residue generating the acylation
stimulating protein (ASP). Levels of ASP are increased in
adipocytes in the postprandial period and by dietary chylomicrons
(By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P01024}.
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EMBL; AM086793; CAJ31249.1; -; Genomic_DNA.
EMBL; BC112452; AAI12453.1; -; mRNA.
RefSeq; NP_001035559.2; NM_001040469.2.
RefSeq; XP_010805188.1; XM_010806886.2.
UniGene; Bt.19562; -.
PDB; 2B39; X-ray; 3.00 A; A/B=1-1661.
PDBsum; 2B39; -.
SMR; Q2UVX4; -.
STRING; 9913.ENSBTAP00000022979; -.
MEROPS; I39.950; -.
PaxDb; Q2UVX4; -.
PeptideAtlas; Q2UVX4; -.
PRIDE; Q2UVX4; -.
GeneID; 280677; -.
KEGG; bta:280677; -.
CTD; 718; -.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
HOGENOM; HOG000286028; -.
HOVERGEN; HBG005110; -.
InParanoid; Q2UVX4; -.
KO; K03990; -.
EvolutionaryTrace; Q2UVX4; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
GO; GO:0010828; P:positive regulation of glucose transport; ISS:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:UniProtKB.
CDD; cd03583; NTR_complement_C3; 1.
Gene3D; 1.20.91.20; -; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.60.40.690; -; 1.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011626; A2M_comp.
InterPro; IPR002890; A2M_N.
InterPro; IPR011625; A2M_N_2.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR035711; Complement_C3-like.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR019742; MacrogloblnA2_CS.
InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR035815; NTR_complement_C3.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
Pfam; PF00207; A2M; 1.
Pfam; PF07678; A2M_comp; 1.
Pfam; PF01835; A2M_N; 1.
Pfam; PF07703; A2M_N_2; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01759; NTR; 1.
Pfam; PF10569; Thiol-ester_cl; 1.
PRINTS; PR00004; ANAPHYLATOXN.
SMART; SM01360; A2M; 1.
SMART; SM01359; A2M_N_2; 1.
SMART; SM01361; A2M_recep; 1.
SMART; SM00104; ANATO; 1.
SMART; SM00643; C345C; 1.
SUPFAM; SSF47686; SSF47686; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF49410; SSF49410; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PROSITE; PS50189; NTR; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues;
Complement alternate pathway; Complement pathway; Complete proteome;
Disulfide bond; Fatty acid metabolism; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Lipid metabolism;
Phosphoprotein; Reference proteome; Secreted; Signal; Thioester bond.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1661 Complement C3.
/FTId=PRO_0000236227.
CHAIN 23 665 Complement C3 beta chain. {ECO:0000250}.
/FTId=PRO_0000236228.
CHAIN 567 665 C3-beta-c. {ECO:0000250}.
/FTId=PRO_0000430428.
CHAIN 670 1661 Complement C3 alpha chain. {ECO:0000250}.
/FTId=PRO_0000236229.
CHAIN 670 746 C3a anaphylatoxin. {ECO:0000250}.
/FTId=PRO_0000236230.
CHAIN 670 745 Acylation stimulating protein.
{ECO:0000250}.
/FTId=PRO_0000419934.
CHAIN 747 1661 Complement C3b alpha' chain.
{ECO:0000250}.
/FTId=PRO_0000236231.
CHAIN 747 953 Complement C3c alpha' chain fragment 1.
{ECO:0000250}.
/FTId=PRO_0000273938.
CHAIN 954 1302 Complement C3dg fragment. {ECO:0000250}.
/FTId=PRO_0000273939.
CHAIN 954 1000 Complement C3g fragment. {ECO:0000250}.
/FTId=PRO_0000273940.
CHAIN 1001 1302 Complement C3d fragment. {ECO:0000250}.
/FTId=PRO_0000236232.
PEPTIDE 1303 1319 Complement C3f fragment. {ECO:0000250}.
/FTId=PRO_0000273941.
CHAIN 1320 1661 Complement C3c alpha' chain fragment 2.
{ECO:0000250}.
/FTId=PRO_0000273942.
DOMAIN 691 726 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1516 1659 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 1423 1454 Properdin-binding. {ECO:0000250}.
SITE 745 746 Cleavage; by carboxypeptidases.
{ECO:0000250}.
SITE 746 747 Cleavage; by C3 convertase.
{ECO:0000250}.
SITE 953 954 Cleavage; by factor I. {ECO:0000250}.
SITE 1302 1303 Cleavage; by factor I. {ECO:0000250}.
SITE 1319 1320 Cleavage; by factor I. {ECO:0000250}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 967 967 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1320 1320 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1571 1571 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
CARBOHYD 938 938 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1649 1649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 557 815 Interchain (between beta and alpha
chains). {ECO:0000255|PROSITE-
ProRule:PRU00022, ECO:0000255|PROSITE-
ProRule:PRU00295}.
DISULFID 625 660 {ECO:0000250}.
DISULFID 691 718 {ECO:0000250}.
DISULFID 692 725 {ECO:0000250}.
DISULFID 705 726 {ECO:0000250}.
DISULFID 872 1511 {ECO:0000250}.
DISULFID 1100 1157 {ECO:0000250}.
DISULFID 1357 1487 {ECO:0000250}.
DISULFID 1388 1456 {ECO:0000250}.
DISULFID 1504 1509 {ECO:0000250}.
DISULFID 1516 1588 {ECO:0000250}.
DISULFID 1535 1659 {ECO:0000250}.
DISULFID 1635 1644 {ECO:0000250}.
CROSSLNK 1009 1012 Isoglutamyl cysteine thioester (Cys-Gln).
{ECO:0000250}.
CONFLICT 533 533 Y -> N (in Ref. 2; AAI12453).
{ECO:0000305}.
CONFLICT 747 747 S -> I (in Ref. 2; AAI12453).
{ECO:0000305}.
STRAND 31 34 {ECO:0000244|PDB:2B39}.
STRAND 38 45 {ECO:0000244|PDB:2B39}.
STRAND 51 54 {ECO:0000244|PDB:2B39}.
STRAND 62 64 {ECO:0000244|PDB:2B39}.
STRAND 75 77 {ECO:0000244|PDB:2B39}.
TURN 78 81 {ECO:0000244|PDB:2B39}.
STRAND 82 89 {ECO:0000244|PDB:2B39}.
STRAND 105 111 {ECO:0000244|PDB:2B39}.
STRAND 114 122 {ECO:0000244|PDB:2B39}.
STRAND 128 134 {ECO:0000244|PDB:2B39}.
STRAND 136 138 {ECO:0000244|PDB:2B39}.
STRAND 142 151 {ECO:0000244|PDB:2B39}.
STRAND 162 168 {ECO:0000244|PDB:2B39}.
STRAND 171 179 {ECO:0000244|PDB:2B39}.
TURN 181 185 {ECO:0000244|PDB:2B39}.
STRAND 189 193 {ECO:0000244|PDB:2B39}.
STRAND 201 209 {ECO:0000244|PDB:2B39}.
STRAND 212 223 {ECO:0000244|PDB:2B39}.
STRAND 234 236 {ECO:0000244|PDB:2B39}.
STRAND 238 241 {ECO:0000244|PDB:2B39}.
STRAND 252 255 {ECO:0000244|PDB:2B39}.
STRAND 257 261 {ECO:0000244|PDB:2B39}.
STRAND 266 275 {ECO:0000244|PDB:2B39}.
HELIX 284 286 {ECO:0000244|PDB:2B39}.
STRAND 288 295 {ECO:0000244|PDB:2B39}.
STRAND 297 299 {ECO:0000244|PDB:2B39}.
TURN 303 306 {ECO:0000244|PDB:2B39}.
STRAND 307 309 {ECO:0000244|PDB:2B39}.
HELIX 314 317 {ECO:0000244|PDB:2B39}.
STRAND 318 320 {ECO:0000244|PDB:2B39}.
STRAND 324 331 {ECO:0000244|PDB:2B39}.
TURN 332 334 {ECO:0000244|PDB:2B39}.
STRAND 351 353 {ECO:0000244|PDB:2B39}.
STRAND 356 358 {ECO:0000244|PDB:2B39}.
STRAND 361 363 {ECO:0000244|PDB:2B39}.
STRAND 365 370 {ECO:0000244|PDB:2B39}.
TURN 378 380 {ECO:0000244|PDB:2B39}.
STRAND 388 390 {ECO:0000244|PDB:2B39}.
STRAND 400 402 {ECO:0000244|PDB:2B39}.
STRAND 408 411 {ECO:0000244|PDB:2B39}.
STRAND 418 424 {ECO:0000244|PDB:2B39}.
STRAND 427 429 {ECO:0000244|PDB:2B39}.
STRAND 437 443 {ECO:0000244|PDB:2B39}.
HELIX 447 449 {ECO:0000244|PDB:2B39}.
STRAND 453 457 {ECO:0000244|PDB:2B39}.
STRAND 468 476 {ECO:0000244|PDB:2B39}.
TURN 479 481 {ECO:0000244|PDB:2B39}.
HELIX 482 484 {ECO:0000244|PDB:2B39}.
STRAND 487 493 {ECO:0000244|PDB:2B39}.
STRAND 495 505 {ECO:0000244|PDB:2B39}.
STRAND 513 518 {ECO:0000244|PDB:2B39}.
HELIX 521 523 {ECO:0000244|PDB:2B39}.
STRAND 527 533 {ECO:0000244|PDB:2B39}.
STRAND 545 551 {ECO:0000244|PDB:2B39}.
STRAND 562 567 {ECO:0000244|PDB:2B39}.
STRAND 578 585 {ECO:0000244|PDB:2B39}.
STRAND 590 596 {ECO:0000244|PDB:2B39}.
HELIX 598 601 {ECO:0000244|PDB:2B39}.
HELIX 605 607 {ECO:0000244|PDB:2B39}.
HELIX 611 618 {ECO:0000244|PDB:2B39}.
STRAND 621 623 {ECO:0000244|PDB:2B39}.
HELIX 632 639 {ECO:0000244|PDB:2B39}.
STRAND 646 648 {ECO:0000244|PDB:2B39}.
HELIX 672 682 {ECO:0000244|PDB:2B39}.
HELIX 688 694 {ECO:0000244|PDB:2B39}.
HELIX 705 708 {ECO:0000244|PDB:2B39}.
HELIX 709 711 {ECO:0000244|PDB:2B39}.
HELIX 716 736 {ECO:0000244|PDB:2B39}.
TURN 756 758 {ECO:0000244|PDB:2B39}.
STRAND 769 774 {ECO:0000244|PDB:2B39}.
STRAND 786 793 {ECO:0000244|PDB:2B39}.
STRAND 799 805 {ECO:0000244|PDB:2B39}.
STRAND 807 809 {ECO:0000244|PDB:2B39}.
TURN 810 812 {ECO:0000244|PDB:2B39}.
STRAND 813 815 {ECO:0000244|PDB:2B39}.
STRAND 820 823 {ECO:0000244|PDB:2B39}.
STRAND 827 833 {ECO:0000244|PDB:2B39}.
STRAND 838 841 {ECO:0000244|PDB:2B39}.
STRAND 843 852 {ECO:0000244|PDB:2B39}.
STRAND 859 865 {ECO:0000244|PDB:2B39}.
STRAND 882 887 {ECO:0000244|PDB:2B39}.
STRAND 892 901 {ECO:0000244|PDB:2B39}.
STRAND 905 920 {ECO:0000244|PDB:2B39}.
STRAND 922 931 {ECO:0000244|PDB:2B39}.
STRAND 933 946 {ECO:0000244|PDB:2B39}.
HELIX 948 951 {ECO:0000244|PDB:2B39}.
STRAND 953 955 {ECO:0000244|PDB:2B39}.
STRAND 957 961 {ECO:0000244|PDB:2B39}.
STRAND 967 969 {ECO:0000244|PDB:2B39}.
STRAND 976 984 {ECO:0000244|PDB:2B39}.
HELIX 987 993 {ECO:0000244|PDB:2B39}.
TURN 996 998 {ECO:0000244|PDB:2B39}.
HELIX 999 1001 {ECO:0000244|PDB:2B39}.
STRAND 1002 1005 {ECO:0000244|PDB:2B39}.
HELIX 1012 1016 {ECO:0000244|PDB:2B39}.
HELIX 1018 1030 {ECO:0000244|PDB:2B39}.
HELIX 1033 1035 {ECO:0000244|PDB:2B39}.
HELIX 1040 1056 {ECO:0000244|PDB:2B39}.
HELIX 1075 1088 {ECO:0000244|PDB:2B39}.
TURN 1089 1091 {ECO:0000244|PDB:2B39}.
HELIX 1096 1109 {ECO:0000244|PDB:2B39}.
HELIX 1140 1152 {ECO:0000244|PDB:2B39}.
TURN 1153 1160 {ECO:0000244|PDB:2B39}.
HELIX 1164 1178 {ECO:0000244|PDB:2B39}.
TURN 1179 1181 {ECO:0000244|PDB:2B39}.
HELIX 1185 1197 {ECO:0000244|PDB:2B39}.
HELIX 1203 1212 {ECO:0000244|PDB:2B39}.
TURN 1215 1217 {ECO:0000244|PDB:2B39}.
HELIX 1225 1242 {ECO:0000244|PDB:2B39}.
TURN 1245 1247 {ECO:0000244|PDB:2B39}.
HELIX 1249 1257 {ECO:0000244|PDB:2B39}.
HELIX 1268 1284 {ECO:0000244|PDB:2B39}.
HELIX 1288 1290 {ECO:0000244|PDB:2B39}.
STRAND 1296 1298 {ECO:0000244|PDB:2B39}.
STRAND 1300 1304 {ECO:0000244|PDB:2B39}.
STRAND 1310 1315 {ECO:0000244|PDB:2B39}.
STRAND 1317 1321 {ECO:0000244|PDB:2B39}.
STRAND 1329 1333 {ECO:0000244|PDB:2B39}.
STRAND 1339 1349 {ECO:0000244|PDB:2B39}.
STRAND 1358 1368 {ECO:0000244|PDB:2B39}.
STRAND 1382 1391 {ECO:0000244|PDB:2B39}.
STRAND 1393 1395 {ECO:0000244|PDB:2B39}.
STRAND 1399 1405 {ECO:0000244|PDB:2B39}.
STRAND 1410 1412 {ECO:0000244|PDB:2B39}.
HELIX 1414 1422 {ECO:0000244|PDB:2B39}.
STRAND 1423 1425 {ECO:0000244|PDB:2B39}.
STRAND 1429 1439 {ECO:0000244|PDB:2B39}.
STRAND 1441 1447 {ECO:0000244|PDB:2B39}.
STRAND 1451 1453 {ECO:0000244|PDB:2B39}.
STRAND 1455 1463 {ECO:0000244|PDB:2B39}.
STRAND 1465 1469 {ECO:0000244|PDB:2B39}.
STRAND 1473 1479 {ECO:0000244|PDB:2B39}.
STRAND 1485 1491 {ECO:0000244|PDB:2B39}.
HELIX 1506 1511 {ECO:0000244|PDB:2B39}.
TURN 1512 1516 {ECO:0000244|PDB:2B39}.
TURN 1529 1534 {ECO:0000244|PDB:2B39}.
STRAND 1539 1551 {ECO:0000244|PDB:2B39}.
STRAND 1554 1566 {ECO:0000244|PDB:2B39}.
STRAND 1576 1578 {ECO:0000244|PDB:2B39}.
STRAND 1581 1585 {ECO:0000244|PDB:2B39}.
TURN 1586 1588 {ECO:0000244|PDB:2B39}.
HELIX 1589 1592 {ECO:0000244|PDB:2B39}.
STRAND 1599 1606 {ECO:0000244|PDB:2B39}.
HELIX 1633 1636 {ECO:0000244|PDB:2B39}.
HELIX 1639 1646 {ECO:0000244|PDB:2B39}.
HELIX 1647 1649 {ECO:0000244|PDB:2B39}.
TURN 1650 1653 {ECO:0000244|PDB:2B39}.
STRAND 1654 1656 {ECO:0000244|PDB:2B39}.
SEQUENCE 1661 AA; 187253 MW; 3EBBE948F0638AD2 CRC64;
MKPTSGPSLL LLLLASLPMA LGNPMYSMIT PNILRLESEE TVVLEAHGGQ GTIQVSVTVH
DFPAKKQVLS NENTQLNSNN GYLSTVTIKI PASKELKSDK GHKFVTVVAT FGNVQVEKVV
LISLQSGYLF IQTDKTIYTP GSTVLYRVFT VDHKLLPVGQ TVFITIETPD GIPVKRDSKS
SQNQFGILTL SWNIPELVNM GVWKIKAYYE DSPQQVFSAE FEVKEYVLPS FEVQLEPEEK
FYYIDDPDGL KVNIIARFLY GEQVDGTAFV IFGVQDGDRR ISLTHSLTRV PINDGNGEAI
LKRQVLLNGV QPSRADALVG KSIYVSATVI LQSGSDMVEA ERTGIPIVTS PYQIHFTKTP
KFFKPAMPFD LMVYVTNPDG SPARHIPVVT QGSNVQSLTQ DDGVAKLSIN TQNKRDPLTI
TVRTKKDNIP EGRQATRTMQ ALPYNTQGNS NNYLHLSVPR VELKPGETLN VNFHLRTDPG
EQAKIRYYTY MIMNKGKLLK VGRQYREPGQ DLVVLPLTIT SDFIPSFRLV AYYTLINAKG
QREVVADSVW VDVKDSCMGT LVVKNGGKEE KHHRPGQQIT LKIEADQGAR VGLVAVDKGV
FVLNKKNKLT QRKIWDVVEK ADIGCTPGSG RNYAGVFTDA GLTLKTSQGL ETQQRADPQC
PQPATRRRRS VQLMEKRMDK AGQYSSDLRK CCEDGMRDNP MKFPCQRRAQ FILQGDACVK
AFLDCCEYIT QLRQQHSRDG ALELARSDLD DDIIPEEDII SRSQFPESWL WTVIEDLKQA
DKNGISTKLM NVFLKDSITT WEILAVSLSD KKGICVADPY EVTVMQDFFI DLRLPYSVVR
NEQVEIRAIL YNYREAENLK VRVELLYNPA FCSLATAKKR HQQTITIPAR SSVAVPYVIV
PLKIGLHEVE VKAAVYNHFI SDGVKKTLKV VPEGVRVNKT VAVRTLNPEH LGQGGVQREE
VPAADLSDQV PDTESETKIL LQGTPVAQMT EDAIDGERLK HLIQTPSGCG EQNMIGMTPT
VIAVHYLDST DQWEKFGLEK RQESLELIRK GYTQQLAFRQ KSSAYAAFQY RPPSTWLTAY
VVKVFALAAN LIAIDSKDLC ETVKWLILEK QKPDGIFQED GPVIHQEMIG GFRDTREKDV
SLTAFVLIAL HEAKDICEAQ VNSLGRSIAK AGDFLENHYR ELRRPYTVAI AAYALALLGK
LEGDRLTKFL NTAKEKNRWE EPNQKLYNVE ATSYALLALL ARKDYDTTPP VVRWLNEQRY
YGGGYGSTQA TFMVFQALAQ YQKDVPDHKE LNLDVSIQLP SRNSAVRHRI LWESASLLRS
EETKENERFT VKAEGKGQGT LSVVTVYHAK LKGKVSCKKF DLRVSIRPAP ETVKKPQDAK
GSMILDICTK YLGDQDATMS ILDISMMTGF SPDVEDLKTL STGVDRYISK YEMNRDSNKN
TLIIYLDKVS HTVEDCLSFK VHQYFNVGLI QPGAVKVYSY YNLDETCIRF YHPDKEDGML
SKLCHKDTCR CAEENCFMHH TEKEVTLEDR LDKACEPGVD YVYKTRLIQK KLEDDFDEYI
MVIENIIKSG SDEVQVKQER KFISHIKCRE ALKLKEGAHY LVWGVSSDLW GEKPKISYII
GKDTWVELWP EAEECQDEEN QKQCEDLANF TENMVVFGCP N


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