ID ADA22_HUMAN Reviewed; 906 AA. AC Q9P0K1; O75075; O75076; Q9P0K2; Q9UIA1; Q9UKK2; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAY-2015, entry version 143. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 22; DE Short=ADAM 22; DE AltName: Full=Metalloproteinase-disintegrin ADAM22-3; DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2; DE Flags: Precursor; GN Name=ADAM22; Synonyms=MDC2; 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] (ISOFORMS 3 AND 4). RC TISSUE=Brain; RX PubMed=9693107; RA Sagane K., Ohya Y., Hasegawa Y., Tanaka I.; RT "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 RT and MDC3: novel human cellular disintegrins highly expressed in the RT brain."; RL Biochem. J. 334:93-98(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=11050470; RA Harada T., Nishie A., Torigoe K., Ikezaki K., Shono T., Maehara Y., RA Kuwano M., Wada M.; RT "The specific expression of three novel splice variant forms of human RT metalloprotease-like disintegrin-like cysteine-rich protein 2 gene in RT brain tissues and gliomas."; RL Jpn. J. Cancer Res. 91:1001-1006(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT ARG-81. RC TISSUE=Brain; RA Wada M., Torigoe K., Harada T., Kuwano M.; RT "Isolation and tissue specific expression of novel ADAM family from RT 7q21.1 region."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-906 (ISOFORM 1), AND VARIANT ARG-81. RC TISSUE=Cerebellum; RX PubMed=10524237; DOI=10.1016/S0378-1119(99)00302-9; RA Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.; RT "The identification of seven metalloproteinase-disintegrin (ADAM) RT genes from genomic libraries."; RL Gene 237:61-70(1999). RN [6] RP FUNCTION, INTERACTION WITH YWHAZ, AND MUTAGENESIS OF SER-834 AND RP SER-857. RX PubMed=12589811; DOI=10.1016/S0006-291X(03)00056-1; RA Zhu P., Sun Y., Xu R., Sang Y., Zhao J., Liu G., Cai L., Li C., RA Zhao S.; RT "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell RT adhesion and spreading."; RL Biochem. Biophys. Res. Commun. 301:991-999(2003). RN [7] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [8] RP FUNCTION, INTERACTION WITH YWHAB, AND MUTAGENESIS OF SER-834 AND RP SER-857. RX PubMed=15882968; DOI=10.1016/j.bbrc.2005.03.229; RA Zhu P., Sang Y., Xu H., Zhao J., Xu R., Sun Y., Xu T., Wang X., RA Chen L., Feng H., Li C., Zhao S.; RT "ADAM22 plays an important role in cell adhesion and spreading with RT the assistance of 14-3-3."; RL Biochem. Biophys. Res. Commun. 331:938-946(2005). RN [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=16385342; DOI=10.1227/01.NEU.0000192363.84287.8B; RA D'Abaco G.M., Ng K., Paradiso L., Godde N.J., Kaye A., Novak U.; RT "ADAM22, expressed in normal brain but not in high-grade gliomas, RT inhibits cellular proliferation via the disintegrin domain."; RL Neurosurgery 58:179-186(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 233-736, GLYCOSYLATION AT RP ASN-519; ASN-634 AND ASN-675, DISULFIDE BONDS, AND FUNCTION. RX PubMed=19692335; DOI=10.1074/jbc.M109.014258; RA Liu H., Shim A.H., He X.; RT "Structural characterization of the ectodomain of a disintegrin and RT metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of RT metalloproteinase: insights on ADAM function."; RL J. Biol. Chem. 284:29077-29086(2009). CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non CC catalytic metalloprotease-like protein (PubMed:19692335). Involved CC in regulation of cell adhesion and spreading and in inhibition of CC cell proliferation. Neuronal receptor for LGI1. CC {ECO:0000269|PubMed:12589811, ECO:0000269|PubMed:15882968, CC ECO:0000269|PubMed:16385342, ECO:0000269|PubMed:19692335}. CC -!- SUBUNIT: Interacts with LGI1 and can bind to LGI4 (By similarity). CC Interacts with KCNA2, DLG2 and DLG4 (By similarity). Interacts CC through its C-terminal region with YWHAB/14-3-3 beta and YWHAZ/14- CC 3-3 zeta but not with YWHAE/14-3-3 epsilon or YWHAH/14-3-3 eta. CC {ECO:0000250|UniProtKB:Q9R1V6, ECO:0000269|PubMed:12589811, CC ECO:0000269|PubMed:15882968}. CC -!- INTERACTION: CC P31946:YWHAB; NbExp=2; IntAct=EBI-1567267, EBI-359815; CC P27348:YWHAQ; NbExp=2; IntAct=EBI-1567267, EBI-359854; CC P63104:YWHAZ; NbExp=3; IntAct=EBI-1567267, EBI-347088; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q9R1V6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=Epsilon; CC IsoId=Q9P0K1-1; Sequence=Displayed; CC Name=2; Synonyms=Delta; CC IsoId=Q9P0K1-2; Sequence=VSP_005482, VSP_005484; 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 Ref.2 (AAF73288) sequence is in conflict in position: 848:G->E. CC {ECO:0000305}; CC Name=3; Synonyms=Alpha; CC IsoId=Q9P0K1-3; Sequence=VSP_005483; CC Name=4; Synonyms=Beta; CC IsoId=Q9P0K1-4; Sequence=VSP_005482, VSP_005483; CC Name=5; CC IsoId=Q9P0K1-5; Sequence=VSP_005482; CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and in some CC high-grade but not low-grade gliomas. Detected slightly or not at CC all in other tissues. {ECO:0000269|PubMed:16385342}. CC -!- PTM: The precursor is cleaved by a furin endopeptidase. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 disintegrin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00068}. CC -!- SIMILARITY: Contains 1 EGF-like domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 peptidase M12B domain. CC {ECO:0000255|PROSITE-ProRule:PRU00276}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB009671; BAA32349.1; -; mRNA. DR EMBL; AB009671; BAA32350.1; -; mRNA. DR EMBL; AF155381; AAF73288.1; -; mRNA. DR EMBL; AF155382; AAF73289.1; -; mRNA. DR EMBL; AF073291; AAF22476.2; -; mRNA. DR EMBL; AC005075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF158637; AAD55251.1; -; mRNA. DR CCDS; CCDS43608.1; -. [Q9P0K1-2] DR CCDS; CCDS43609.1; -. [Q9P0K1-5] DR CCDS; CCDS43610.1; -. [Q9P0K1-3] DR CCDS; CCDS47637.1; -. [Q9P0K1-1] DR RefSeq; NP_004185.1; NM_004194.3. [Q9P0K1-3] DR RefSeq; NP_068367.1; NM_021721.3. [Q9P0K1-4] DR RefSeq; NP_068368.2; NM_021722.4. [Q9P0K1-2] DR RefSeq; NP_068369.1; NM_021723.3. [Q9P0K1-1] DR UniGene; Hs.256398; -. DR PDB; 3G5C; X-ray; 2.36 A; A/B=233-736. DR PDBsum; 3G5C; -. DR ProteinModelPortal; Q9P0K1; -. DR SMR; Q9P0K1; 233-718. DR BioGrid; 119789; 7. DR IntAct; Q9P0K1; 11. DR MINT; MINT-252818; -. DR STRING; 9606.ENSP00000265727; -. DR MEROPS; M12.978; -. DR PhosphoSite; Q9P0K1; -. DR BioMuta; ADAM22; -. DR DMDM; 14423634; -. DR MaxQB; Q9P0K1; -. DR PaxDb; Q9P0K1; -. DR PRIDE; Q9P0K1; -. DR Ensembl; ENST00000265727; ENSP00000265727; ENSG00000008277. [Q9P0K1-1] DR Ensembl; ENST00000398201; ENSP00000381260; ENSG00000008277. [Q9P0K1-3] DR Ensembl; ENST00000398204; ENSP00000381262; ENSG00000008277. [Q9P0K1-5] DR Ensembl; ENST00000398209; ENSP00000381267; ENSG00000008277. [Q9P0K1-2] DR GeneID; 53616; -. DR KEGG; hsa:53616; -. DR UCSC; uc003ujk.2; human. [Q9P0K1-1] DR UCSC; uc003ujl.2; human. [Q9P0K1-4] DR UCSC; uc003ujm.3; human. [Q9P0K1-2] DR UCSC; uc003ujo.3; human. [Q9P0K1-5] DR CTD; 53616; -. DR GeneCards; GC07P087563; -. DR HGNC; HGNC:201; ADAM22. DR HPA; HPA045282; -. DR MIM; 603709; gene. DR neXtProt; NX_Q9P0K1; -. DR PharmGKB; PA24518; -. DR eggNOG; NOG256419; -. DR GeneTree; ENSGT00760000118888; -. DR HOGENOM; HOG000231962; -. DR HOVERGEN; HBG050456; -. DR InParanoid; Q9P0K1; -. DR KO; K16068; -. DR OMA; FSGSQFE; -. DR OrthoDB; EOG7B31M6; -. DR PhylomeDB; Q9P0K1; -. DR TreeFam; TF314733; -. DR ChiTaRS; ADAM22; human. DR EvolutionaryTrace; Q9P0K1; -. DR GeneWiki; ADAM22; -. DR GenomeRNAi; 53616; -. DR NextBio; 56096; -. DR PRO; PR:Q9P0K1; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; Q9P0K1; -. DR CleanEx; HS_ADAM22; -. DR ExpressionAtlas; Q9P0K1; baseline and differential. DR Genevestigator; Q9P0K1; -. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB. DR GO; GO:0005178; F:integrin binding; NAS:UniProtKB. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR GO; GO:0007162; P:negative regulation of cell adhesion; NAS:UniProtKB. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Blood-coag_inhib_Disintegrin. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR000742; EG-like_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SMART; SM00181; EGF; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell projection; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; KW Receptor; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT PROPEP 26 222 {ECO:0000250}. FT /FTId=PRO_0000029112. FT CHAIN 223 906 Disintegrin and metalloproteinase domain- FT containing protein 22. FT /FTId=PRO_0000029113. FT TOPO_DOM 223 736 Extracellular. {ECO:0000255}. FT TRANSMEM 737 757 Helical. {ECO:0000255}. FT TOPO_DOM 758 906 Cytoplasmic. {ECO:0000255}. FT DOMAIN 239 438 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 444 531 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 675 712 EGF-like. FT COMPBIAS 532 678 Cys-rich. FT MOD_RES 834 834 Phosphoserine. FT {ECO:0000269|PubMed:21406692}. FT CARBOHYD 175 175 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 519 519 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19692335}. FT CARBOHYD 634 634 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19692335}. FT CARBOHYD 675 675 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19692335}. FT DISULFID 349 433 {ECO:0000269|PubMed:19692335}. FT DISULFID 392 417 {ECO:0000269|PubMed:19692335}. FT DISULFID 394 401 {ECO:0000269|PubMed:19692335}. FT DISULFID 447 477 {ECO:0000269|PubMed:19692335}. FT DISULFID 458 474 {ECO:0000269|PubMed:19692335}. FT DISULFID 460 466 {ECO:0000269|PubMed:19692335}. FT DISULFID 473 494 {ECO:0000269|PubMed:19692335}. FT DISULFID 485 491 {ECO:0000269|PubMed:19692335}. FT DISULFID 490 516 {ECO:0000269|PubMed:19692335}. FT DISULFID 503 523 {ECO:0000269|PubMed:19692335}. FT DISULFID 510 542 {ECO:0000269|PubMed:19692335}. FT DISULFID 535 547 {ECO:0000269|PubMed:19692335}. FT DISULFID 554 605 {ECO:0000269|PubMed:19692335}. FT DISULFID 569 635 {ECO:0000269|PubMed:19692335}. FT DISULFID 583 593 {ECO:0000269|PubMed:19692335}. FT DISULFID 600 663 {ECO:0000269|PubMed:19692335}. FT DISULFID 657 668 {ECO:0000269|PubMed:19692335}. FT DISULFID 679 694 {ECO:0000269|PubMed:19692335}. FT DISULFID 688 700 {ECO:0000269|PubMed:19692335}. FT DISULFID 702 711 {ECO:0000269|PubMed:19692335}. FT VAR_SEQ 768 803 Missing (in isoform 2, isoform 4 and FT isoform 5). {ECO:0000303|PubMed:11050470, FT ECO:0000303|PubMed:9693107, FT ECO:0000303|Ref.3}. FT /FTId=VSP_005482. FT VAR_SEQ 859 859 E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in FT isoform 2). FT {ECO:0000303|PubMed:11050470}. FT /FTId=VSP_005484. FT VAR_SEQ 860 906 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:9693107}. FT /FTId=VSP_005483. FT VARIANT 81 81 P -> R (in dbSNP:rs2279542). FT {ECO:0000269|PubMed:10524237, FT ECO:0000269|Ref.3}. FT /FTId=VAR_020057. FT VARIANT 119 119 H -> Y (in dbSNP:rs4728730). FT /FTId=VAR_051589. FT VARIANT 207 207 V -> I (in dbSNP:rs17255978). FT /FTId=VAR_051590. FT MUTAGEN 834 834 S->A: Abolishes interactions with YWHAB FT and YWHAZ; when associated with A-857. FT {ECO:0000269|PubMed:12589811, FT ECO:0000269|PubMed:15882968}. FT MUTAGEN 857 857 S->A: Abolishes interactions with YWHAB FT and YWHAZ; when associated with A-834. FT {ECO:0000269|PubMed:12589811, FT ECO:0000269|PubMed:15882968}. FT STRAND 235 237 {ECO:0000244|PDB:3G5C}. FT STRAND 239 247 {ECO:0000244|PDB:3G5C}. FT HELIX 249 253 {ECO:0000244|PDB:3G5C}. FT TURN 254 257 {ECO:0000244|PDB:3G5C}. FT HELIX 259 280 {ECO:0000244|PDB:3G5C}. FT STRAND 281 292 {ECO:0000244|PDB:3G5C}. FT HELIX 305 318 {ECO:0000244|PDB:3G5C}. FT STRAND 325 333 {ECO:0000244|PDB:3G5C}. FT STRAND 336 338 {ECO:0000244|PDB:3G5C}. FT STRAND 341 343 {ECO:0000244|PDB:3G5C}. FT TURN 351 353 {ECO:0000244|PDB:3G5C}. FT STRAND 354 359 {ECO:0000244|PDB:3G5C}. FT HELIX 363 378 {ECO:0000244|PDB:3G5C}. FT HELIX 384 389 {ECO:0000244|PDB:3G5C}. FT HELIX 416 427 {ECO:0000244|PDB:3G5C}. FT HELIX 432 435 {ECO:0000244|PDB:3G5C}. FT HELIX 463 466 {ECO:0000244|PDB:3G5C}. FT TURN 467 473 {ECO:0000244|PDB:3G5C}. FT STRAND 486 488 {ECO:0000244|PDB:3G5C}. FT STRAND 491 496 {ECO:0000244|PDB:3G5C}. FT STRAND 502 504 {ECO:0000244|PDB:3G5C}. FT TURN 536 539 {ECO:0000244|PDB:3G5C}. FT STRAND 540 543 {ECO:0000244|PDB:3G5C}. FT STRAND 546 548 {ECO:0000244|PDB:3G5C}. FT HELIX 550 558 {ECO:0000244|PDB:3G5C}. FT HELIX 567 573 {ECO:0000244|PDB:3G5C}. FT TURN 574 576 {ECO:0000244|PDB:3G5C}. FT STRAND 585 590 {ECO:0000244|PDB:3G5C}. FT HELIX 595 597 {ECO:0000244|PDB:3G5C}. FT STRAND 600 602 {ECO:0000244|PDB:3G5C}. FT STRAND 605 607 {ECO:0000244|PDB:3G5C}. FT STRAND 613 617 {ECO:0000244|PDB:3G5C}. FT STRAND 622 628 {ECO:0000244|PDB:3G5C}. FT STRAND 631 637 {ECO:0000244|PDB:3G5C}. FT STRAND 640 645 {ECO:0000244|PDB:3G5C}. FT STRAND 656 658 {ECO:0000244|PDB:3G5C}. FT STRAND 661 666 {ECO:0000244|PDB:3G5C}. FT STRAND 668 670 {ECO:0000244|PDB:3G5C}. FT HELIX 671 674 {ECO:0000244|PDB:3G5C}. FT HELIX 688 690 {ECO:0000244|PDB:3G5C}. FT STRAND 692 695 {ECO:0000244|PDB:3G5C}. FT STRAND 700 702 {ECO:0000244|PDB:3G5C}. FT STRAND 706 708 {ECO:0000244|PDB:3G5C}. SQ SEQUENCE 906 AA; 100433 MW; 265ECCD0FA6C088B CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI //