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LIM and senescent cell antigen-like-containing domain protein 1 (Particularly interesting new Cys-His protein 1) (PINCH-1) (Renal carcinoma antigen NY-REN-48)

 LIMS1_HUMAN             Reviewed;         325 AA.
P48059; B2RAJ4; B7Z483; B7Z7R3; B7Z907; Q53TE0; Q9BS44;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 181.
RecName: Full=LIM and senescent cell antigen-like-containing domain protein 1;
AltName: Full=Particularly interesting new Cys-His protein 1;
Short=PINCH-1;
AltName: Full=Renal carcinoma antigen NY-REN-48;
Name=LIMS1; Synonyms=PINCH, PINCH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=7517666; DOI=10.1006/bbrc.1994.1822;
Rearden A.;
"A new LIM protein containing an autoepitope homologous to 'senescent
cell antigen'.";
Biochem. Biophys. Res. Commun. 201:1124-1131(1994).
[2]
SEQUENCE REVISION TO C-TERMINUS.
Rearden A.;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5).
TISSUE=Testis, Tongue, and Trachea;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
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).
[6]
PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
INTERACTION WITH NCK2.
PubMed=9843575; DOI=10.1091/mbc.9.12.3367;
Tu Y., Li F., Wu C.;
"Nck-2, a novel Src homology2/3-containing adaptor protein that
interacts with the LIM-only protein PINCH and components of growth
factor receptor kinase-signaling pathways.";
Mol. Biol. Cell 9:3367-3382(1998).
[8]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[9]
INTERACTION WITH ILK AND NCK2, AND SUBCELLULAR LOCATION.
PubMed=10022929; DOI=10.1128/MCB.19.3.2425;
Tu Y., Li F., Goicoechea S., Wu C.;
"The LIM-only protein PINCH directly interacts with integrin-linked
kinase and is recruited to integrin-rich sites in spreading cells.";
Mol. Cell. Biol. 19:2425-2434(1999).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
STRUCTURE BY NMR OF 1-70.
PubMed=11078733; DOI=10.1074/jbc.M007632200;
Velyvis A., Yang Y., Wu C., Qin J.;
"Solution structure of the focal adhesion adaptor PINCH LIM1 domain
and characterization of its interaction with the integrin-linked
kinase ankyrin repeat domain.";
J. Biol. Chem. 276:4932-4939(2001).
[12]
STRUCTURE BY NMR OF 188-251.
PubMed=12794636; DOI=10.1038/nsb938;
Velyvis A., Vaynberg J., Yang Y., Vinogradova O., Zhang Y., Wu C.,
Qin J.;
"Structural and functional insights into PINCH LIM4 domain-mediated
integrin signaling.";
Nat. Struct. Biol. 10:558-564(2003).
[13]
STRUCTURE BY NMR OF 71-190.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the second and third LIM domain of particularly
interesting new Cys-His protein (PINCH).";
Submitted (JUN-2006) to the PDB data bank.
[14]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 6-68 IN COMPLEX WITH ILK, AND
MUTAGENESIS OF PHE-42; HIS-61; ASP-62 AND LEU-66.
PubMed=19074270; DOI=10.1073/pnas.0811415106;
Chiswell B.P., Zhang R., Murphy J.W., Boggon T.J., Calderwood D.A.;
"The structural basis of integrin-linked kinase-PINCH interactions.";
Proc. Natl. Acad. Sci. U.S.A. 105:20677-20682(2008).
[15]
STRUCTURE BY NMR OF 1-70 IN COMPLEX WITH ILK, MUTAGENESIS OF PHE-42
AND ARG-56, AND SUBCELLULAR LOCATION.
PubMed=19117955; DOI=10.1074/jbc.M805319200;
Yang Y., Wang X., Hawkins C.A., Chen K., Vaynberg J., Mao X., Tu Y.,
Zuo X., Wang J., Wang Y.-X., Wu C., Tjandra N., Qin J.;
"Structural basis of focal adhesion localization of LIM-only adaptor
PINCH by integrin-linked kinase.";
J. Biol. Chem. 284:5836-5844(2009).
-!- FUNCTION: Adapter protein in a cytoplasmic complex linking beta-
integrins to the actin cytoskeleton, bridges the complex to cell
surface receptor tyrosine kinases and growth factor receptors.
Involved in the regulation of cell survival, cell proliferation
and cell differentiation.
-!- SUBUNIT: Interacts (via LIM zinc-binding 5) with TGFB1I1 (By
similarity). Interacts with integrin-linked protein kinase 1 (ILK)
via the first LIM domain, and in competition with LIMS2. Part of
the heterotrimeric IPP complex composed of integrin-linked kinase
(ILK), LIMS1 or LIMS2, and PARVA. Interacts with SH3/SH2 adapter
NCK2, thereby linking the complex to cell surface receptors.
{ECO:0000250, ECO:0000269|PubMed:10022929,
ECO:0000269|PubMed:19074270, ECO:0000269|PubMed:19117955,
ECO:0000269|PubMed:9843575}.
-!- INTERACTION:
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-306928, EBI-3957603;
Q13418:ILK; NbExp=10; IntAct=EBI-306928, EBI-747644;
O55222:Ilk (xeno); NbExp=3; IntAct=EBI-306928, EBI-6690138;
O43639:NCK2; NbExp=2; IntAct=EBI-306928, EBI-713635;
Q15404:RSU1; NbExp=4; IntAct=EBI-306928, EBI-1057132;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
membrane; Peripheral membrane protein; Cytoplasmic side.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P48059-1; Sequence=Displayed;
Name=2;
IsoId=P48059-2; Sequence=VSP_042672;
Note=No experimental confirmation available.;
Name=3;
IsoId=P48059-3; Sequence=VSP_043210;
Name=4;
IsoId=P48059-4; Sequence=VSP_043211;
Name=5;
IsoId=P48059-5; Sequence=VSP_043212;
-!- TISSUE SPECIFICITY: Expressed in most tissues except in the brain.
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EMBL; U09284; AAA20086.2; -; mRNA.
EMBL; AK296992; BAH12469.1; -; mRNA.
EMBL; AK302411; BAH13699.1; -; mRNA.
EMBL; AK304260; BAH14143.1; -; mRNA.
EMBL; AK314217; BAG36891.1; -; mRNA.
EMBL; AC010095; AAY14983.1; -; Genomic_DNA.
EMBL; AC012487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005341; AAH05341.1; -; mRNA.
CCDS; CCDS2078.1; -. [P48059-1]
CCDS; CCDS54382.1; -. [P48059-2]
CCDS; CCDS54383.1; -. [P48059-4]
CCDS; CCDS54384.1; -. [P48059-5]
CCDS; CCDS54385.1; -. [P48059-3]
PIR; JC2324; JC2324.
RefSeq; NP_001180411.1; NM_001193482.1. [P48059-4]
RefSeq; NP_001180412.1; NM_001193483.2. [P48059-2]
RefSeq; NP_001180413.1; NM_001193484.1. [P48059-5]
RefSeq; NP_001180414.1; NM_001193485.2. [P48059-3]
RefSeq; NP_001180417.1; NM_001193488.1. [P48059-1]
RefSeq; NP_004978.2; NM_004987.5. [P48059-1]
UniGene; Hs.597715; -.
UniGene; Hs.613268; -.
PDB; 1G47; NMR; -; A=1-70.
PDB; 1NYP; NMR; -; A=188-251.
PDB; 1U5S; NMR; -; B=188-251.
PDB; 2COR; NMR; -; A=125-190.
PDB; 2D8X; NMR; -; A=71-127.
PDB; 2KBX; NMR; -; B=1-70.
PDB; 3F6Q; X-ray; 1.60 A; B=6-68.
PDB; 4HI8; X-ray; 1.20 A; B=6-68.
PDB; 4HI9; X-ray; 1.20 A; B=6-68.
PDBsum; 1G47; -.
PDBsum; 1NYP; -.
PDBsum; 1U5S; -.
PDBsum; 2COR; -.
PDBsum; 2D8X; -.
PDBsum; 2KBX; -.
PDBsum; 3F6Q; -.
PDBsum; 4HI8; -.
PDBsum; 4HI9; -.
ProteinModelPortal; P48059; -.
SMR; P48059; -.
BioGrid; 110175; 37.
DIP; DIP-40671N; -.
IntAct; P48059; 38.
MINT; MINT-5004275; -.
STRING; 9606.ENSP00000446121; -.
iPTMnet; P48059; -.
PhosphoSitePlus; P48059; -.
BioMuta; LIMS1; -.
DMDM; 18266876; -.
OGP; P48059; -.
EPD; P48059; -.
MaxQB; P48059; -.
PaxDb; P48059; -.
PeptideAtlas; P48059; -.
PRIDE; P48059; -.
DNASU; 3987; -.
Ensembl; ENST00000332345; ENSP00000331775; ENSG00000169756. [P48059-1]
Ensembl; ENST00000338045; ENSP00000337598; ENSG00000169756. [P48059-3]
Ensembl; ENST00000393310; ENSP00000376987; ENSG00000169756. [P48059-1]
Ensembl; ENST00000409441; ENSP00000387264; ENSG00000169756. [P48059-5]
Ensembl; ENST00000410093; ENSP00000386926; ENSG00000169756. [P48059-4]
Ensembl; ENST00000544547; ENSP00000437912; ENSG00000169756. [P48059-2]
GeneID; 3987; -.
KEGG; hsa:3987; -.
UCSC; uc002teg.4; human. [P48059-1]
CTD; 3987; -.
DisGeNET; 3987; -.
EuPathDB; HostDB:ENSG00000169756.16; -.
GeneCards; LIMS1; -.
HGNC; HGNC:6616; LIMS1.
HPA; HPA058455; -.
HPA; HPA061230; -.
MIM; 602567; gene.
neXtProt; NX_P48059; -.
OpenTargets; ENSG00000169756; -.
PharmGKB; PA30389; -.
eggNOG; KOG2272; Eukaryota.
eggNOG; ENOG410XP46; LUCA.
GeneTree; ENSGT00760000118910; -.
HOGENOM; HOG000253950; -.
HOVERGEN; HBG000053; -.
InParanoid; P48059; -.
OMA; CRECNER; -.
OrthoDB; EOG091G08K3; -.
PhylomeDB; P48059; -.
TreeFam; TF314113; -.
Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
ChiTaRS; LIMS1; human.
EvolutionaryTrace; P48059; -.
GeneWiki; LIMS1; -.
GenomeRNAi; 3987; -.
PRO; PR:P48059; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000169756; -.
CleanEx; HS_LIMS1; -.
ExpressionAtlas; P48059; baseline and differential.
Genevisible; P48059; HS.
GO; GO:0005911; C:cell-cell junction; IMP:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007569; P:cell aging; TAS:ProtInc.
GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:CAFA.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:CAFA.
InterPro; IPR017351; PINCH.
InterPro; IPR001781; Znf_LIM.
PANTHER; PTHR24210; PTHR24210; 1.
Pfam; PF00412; LIM; 5.
PIRSF; PIRSF038003; PINCH; 1.
SMART; SM00132; LIM; 5.
PROSITE; PS00478; LIM_DOMAIN_1; 4.
PROSITE; PS50023; LIM_DOMAIN_2; 5.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Cell membrane; Complete proteome; Direct protein sequencing;
LIM domain; Membrane; Metal-binding; Reference proteome; Repeat; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801}.
CHAIN 2 325 LIM and senescent cell antigen-like-
containing domain protein 1.
/FTId=PRO_0000075888.
DOMAIN 10 62 LIM zinc-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 71 121 LIM zinc-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 135 184 LIM zinc-binding 3. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 193 243 LIM zinc-binding 4. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 252 303 LIM zinc-binding 5. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:12665801}.
VAR_SEQ 1 1 M -> MLGVAAGMTHSNM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042672.
VAR_SEQ 1 1 M -> MAFSGRARPCIIPENEEIPRAALNTVHEANGTEDER
AVSKLQRRHSDVKVYKEFCDFYAKFNM (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_043210.
VAR_SEQ 1 1 M -> MTCNM (in isoform 4). {ECO:0000305}.
/FTId=VSP_043211.
VAR_SEQ 1 1 M -> MTALQLKELSHSGLYRRRRDRPDSLRVNGLPEEELS
NM (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043212.
MUTAGEN 42 42 F->A: Loss of interaction with ILK and
loss of localization to focal adhesion.
{ECO:0000269|PubMed:19074270,
ECO:0000269|PubMed:19117955}.
MUTAGEN 56 56 R->A: Alters interaction with ILK.
{ECO:0000269|PubMed:19117955}.
MUTAGEN 61 61 H->D: Alters interaction with ILK.
{ECO:0000269|PubMed:19074270}.
MUTAGEN 62 62 D->A: Alters interaction with ILK.
{ECO:0000269|PubMed:19074270}.
MUTAGEN 66 66 L->D: Alters interaction with ILK.
{ECO:0000269|PubMed:19074270}.
CONFLICT 78 78 I -> T (in Ref. 5; AAH05341).
{ECO:0000305}.
CONFLICT 262 262 D -> G (in Ref. 5; AAH05341).
{ECO:0000305}.
TURN 11 13 {ECO:0000244|PDB:4HI8}.
STRAND 22 26 {ECO:0000244|PDB:4HI8}.
STRAND 29 32 {ECO:0000244|PDB:4HI8}.
TURN 33 35 {ECO:0000244|PDB:4HI8}.
TURN 39 41 {ECO:0000244|PDB:4HI8}.
HELIX 46 48 {ECO:0000244|PDB:4HI8}.
STRAND 51 53 {ECO:0000244|PDB:4HI8}.
STRAND 56 58 {ECO:0000244|PDB:4HI8}.
HELIX 60 66 {ECO:0000244|PDB:4HI8}.
STRAND 72 74 {ECO:0000244|PDB:2D8X}.
STRAND 83 85 {ECO:0000244|PDB:2D8X}.
STRAND 88 90 {ECO:0000244|PDB:2D8X}.
TURN 92 94 {ECO:0000244|PDB:2D8X}.
STRAND 98 100 {ECO:0000244|PDB:2D8X}.
STRAND 105 107 {ECO:0000244|PDB:2D8X}.
STRAND 110 112 {ECO:0000244|PDB:2D8X}.
STRAND 115 117 {ECO:0000244|PDB:2D8X}.
HELIX 119 126 {ECO:0000244|PDB:2D8X}.
TURN 136 138 {ECO:0000244|PDB:2COR}.
STRAND 150 152 {ECO:0000244|PDB:2COR}.
TURN 156 158 {ECO:0000244|PDB:2COR}.
STRAND 162 164 {ECO:0000244|PDB:2COR}.
STRAND 173 175 {ECO:0000244|PDB:2COR}.
STRAND 178 180 {ECO:0000244|PDB:2COR}.
HELIX 182 186 {ECO:0000244|PDB:2COR}.
TURN 194 197 {ECO:0000244|PDB:1NYP}.
STRAND 210 213 {ECO:0000244|PDB:1NYP}.
TURN 214 216 {ECO:0000244|PDB:1NYP}.
TURN 220 222 {ECO:0000244|PDB:1NYP}.
STRAND 227 229 {ECO:0000244|PDB:1NYP}.
STRAND 232 234 {ECO:0000244|PDB:1NYP}.
STRAND 237 239 {ECO:0000244|PDB:1NYP}.
HELIX 241 247 {ECO:0000244|PDB:1NYP}.
SEQUENCE 325 AA; 37251 MW; E665FEB11D849CAE CRC64;
MANALASATC ERCKGGFAPA EKIVNSNGEL YHEQCFVCAQ CFQQFPEGLF YEFEGRKYCE
HDFQMLFAPC CHQCGEFIIG RVIKAMNNSW HPECFRCDLC QEVLADIGFV KNAGRHLCRP
CHNREKARGL GKYICQKCHA IIDEQPLIFK NDPYHPDHFN CANCGKELTA DARELKGELY
CLPCHDKMGV PICGACRRPI EGRVVNAMGK QWHVEHFVCA KCEKPFLGHR HYERKGLAYC
ETHYNQLFGD VCFHCNRVIE GDVVSALNKA WCVNCFACST CNTKLTLKNK FVEFDMKPVC
KKCYEKFPLE LKKRLKKLAE TLGRK


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