ID   CASS4_HUMAN             Reviewed;         786 AA.
AC   Q9NQ75; E1P5Z8; Q5QPD6; Q96K09; Q9BYL5;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Cas scaffolding protein family member 4;
DE   AltName: Full=HEF-like protein;
DE   AltName: Full=HEF1-EFS-p130Cas-like protein;
DE            Short=HEPL;
GN   Name=CASS4; Synonyms=C20orf32, HEFL;
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] (ISOFORM 1).
RA   Jahn T., Will T., Bresolin G., Coutinho S., Peschel C., Duyster J.;
RT   "HEF-like protein (HEFL) is involved in integrin signalling.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT SER-660.
RC   TISSUE=Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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] (ISOFORM 2).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-249 AND SER-305, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [7]
RP   FUNCTION, INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND PHOSPHORYLATION BY SRC.
RX   PubMed=18256281; DOI=10.1091/mbc.e07-09-0953;
RA   Singh M.K., Dadke D., Nicolas E., Serebriiskii I.G., Apostolou S.,
RA   Canutescu A., Egleston B.L., Golemis E.A.;
RT   "A novel Cas family member, HEPL, regulates FAK and cell spreading.";
RL   Mol. Biol. Cell 19:1627-1636(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-249; SER-305;
RP   SER-376 AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   STRUCTURE BY NMR OF 14-71.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-036, an SH3 domain from human.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Docking protein that plays a role in tyrosine kinase-based
CC       signaling related to cell adhesion and cell spreading. Regulates
CC       PTK2/FAK1 activity, focal adhesion integrity, and cell spreading.
CC       {ECO:0000269|PubMed:18256281}.
CC   -!- SUBUNIT: Interacts (via SH3 domain) with PTK2/FAK1 (via C-terminus).
CC       {ECO:0000269|PubMed:18256281}.
CC   -!- INTERACTION:
CC       Q9NQ75-2; Q7Z6G8-3: ANKS1B; NbExp=3; IntAct=EBI-12270182, EBI-17714371;
CC       Q9NQ75-2; O14613: CDC42EP2; NbExp=4; IntAct=EBI-12270182, EBI-3438291;
CC       Q9NQ75-2; Q13643: FHL3; NbExp=5; IntAct=EBI-12270182, EBI-741101;
CC       Q9NQ75-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12270182, EBI-618309;
CC       Q9NQ75-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-12270182, EBI-7116203;
CC       Q9NQ75-2; Q8TDZ2: MICAL1; NbExp=2; IntAct=EBI-12270182, EBI-7153876;
CC       Q9NQ75-2; Q15942: ZYX; NbExp=4; IntAct=EBI-12270182, EBI-444225;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:18256281}. Cell junction, focal adhesion
CC       {ECO:0000269|PubMed:18256281}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q9NQ75-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NQ75-2; Sequence=VSP_003807;
CC       Name=3;
CC         IsoId=Q9NQ75-3; Sequence=VSP_003806;
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in lung and spleen. Also
CC       highly expressed in ovarian and leukemia cell lines.
CC       {ECO:0000269|PubMed:18256281}.
CC   -!- PTM: Phosphorylated on tyrosines by SRC. {ECO:0000269|PubMed:18256281}.
CC   -!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC00655.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ276678; CAC00655.1; ALT_FRAME; mRNA.
DR   EMBL; AK027760; BAB55351.1; -; mRNA.
DR   EMBL; AL121914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75546.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75547.1; -; Genomic_DNA.
DR   EMBL; BC027951; AAH27951.1; -; mRNA.
DR   CCDS; CCDS33492.1; -. [Q9NQ75-1]
DR   CCDS; CCDS54475.1; -. [Q9NQ75-3]
DR   RefSeq; NP_001157586.1; NM_001164114.1.
DR   RefSeq; NP_001157587.1; NM_001164115.1. [Q9NQ75-3]
DR   RefSeq; NP_001157588.1; NM_001164116.1. [Q9NQ75-1]
DR   RefSeq; NP_065089.2; NM_020356.3. [Q9NQ75-1]
DR   PDB; 2CRE; NMR; -; A=14-71.
DR   PDBsum; 2CRE; -.
DR   AlphaFoldDB; Q9NQ75; -.
DR   SMR; Q9NQ75; -.
DR   BioGRID; 121359; 9.
DR   IntAct; Q9NQ75; 37.
DR   STRING; 9606.ENSP00000353462; -.
DR   GlyGen; Q9NQ75; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NQ75; -.
DR   PhosphoSitePlus; Q9NQ75; -.
DR   BioMuta; CASS4; -.
DR   DMDM; 23813906; -.
DR   EPD; Q9NQ75; -.
DR   MassIVE; Q9NQ75; -.
DR   MaxQB; Q9NQ75; -.
DR   PaxDb; 9606-ENSP00000353462; -.
DR   PeptideAtlas; Q9NQ75; -.
DR   ProteomicsDB; 82093; -. [Q9NQ75-1]
DR   ProteomicsDB; 82094; -. [Q9NQ75-2]
DR   ProteomicsDB; 82095; -. [Q9NQ75-3]
DR   ABCD; Q9NQ75; 2 sequenced antibodies.
DR   Antibodypedia; 2766; 85 antibodies from 20 providers.
DR   DNASU; 57091; -.
DR   Ensembl; ENST00000360314.7; ENSP00000353462.3; ENSG00000087589.17. [Q9NQ75-1]
DR   Ensembl; ENST00000434344.2; ENSP00000410027.1; ENSG00000087589.17. [Q9NQ75-3]
DR   Ensembl; ENST00000679887.1; ENSP00000506506.1; ENSG00000087589.17. [Q9NQ75-1]
DR   GeneID; 57091; -.
DR   KEGG; hsa:57091; -.
DR   MANE-Select; ENST00000679887.1; ENSP00000506506.1; NM_020356.4; NP_065089.2.
DR   UCSC; uc002xxp.3; human. [Q9NQ75-1]
DR   AGR; HGNC:15878; -.
DR   CTD; 57091; -.
DR   DisGeNET; 57091; -.
DR   GeneCards; CASS4; -.
DR   HGNC; HGNC:15878; CASS4.
DR   HPA; ENSG00000087589; Tissue enhanced (lung, lymphoid tissue).
DR   MIM; 618888; gene.
DR   neXtProt; NX_Q9NQ75; -.
DR   NIAGADS; ENSG00000087589; -.
DR   OpenTargets; ENSG00000087589; -.
DR   PharmGKB; PA162381095; -.
DR   VEuPathDB; HostDB:ENSG00000087589; -.
DR   eggNOG; ENOG502QUJM; Eukaryota.
DR   GeneTree; ENSGT00950000183008; -.
DR   HOGENOM; CLU_017000_0_1_1; -.
DR   InParanoid; Q9NQ75; -.
DR   OMA; TYERMDM; -.
DR   OrthoDB; 2902504at2759; -.
DR   PhylomeDB; Q9NQ75; -.
DR   TreeFam; TF328782; -.
DR   PathwayCommons; Q9NQ75; -.
DR   SignaLink; Q9NQ75; -.
DR   BioGRID-ORCS; 57091; 16 hits in 1151 CRISPR screens.
DR   ChiTaRS; CASS4; human.
DR   EvolutionaryTrace; Q9NQ75; -.
DR   GenomeRNAi; 57091; -.
DR   Pharos; Q9NQ75; Tbio.
DR   PRO; PR:Q9NQ75; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9NQ75; Protein.
DR   Bgee; ENSG00000087589; Expressed in upper lobe of left lung and 96 other cell types or tissues.
DR   ExpressionAtlas; Q9NQ75; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:ARUK-UCL.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd11568; FAT-like_CASS4_C; 1.
DR   CDD; cd11551; Serine_rich_CASS4; 1.
DR   CDD; cd12000; SH3_CASS4; 1.
DR   Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1.
DR   Gene3D; 1.20.120.830; Serine-rich domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR021901; CAS_C.
DR   InterPro; IPR037362; CAS_fam.
DR   InterPro; IPR035744; CASS4_SH3.
DR   InterPro; IPR014928; Serine_rich_dom.
DR   InterPro; IPR038319; Serine_rich_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR   PANTHER; PTHR10654:SF19; CAS SCAFFOLDING PROTEIN FAMILY MEMBER 4; 1.
DR   Pfam; PF12026; CAS_C; 1.
DR   Pfam; PF08824; Serine_rich; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q9NQ75; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..786
FT                   /note="Cas scaffolding protein family member 4"
FT                   /id="PRO_0000079425"
FT   DOMAIN          11..73
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          262..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         215..651
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_003806"
FT   VAR_SEQ         652..786
FT                   /note="NPGPLIPQPSSQQTPERKPRLSEHCRLYFGALFKAISAFHGSLSSSQPAEII
FT                   TQSKLVIMVGQKLVDTLCMETQERDVRNEILRGSSHLCSLLKDVALATKNAVLTYPSPA
FT                   ALGHLQAEAEKLEQHTRQFRGTLG -> VSSEFQVIEKGASIVTWSSGY (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003807"
FT   VARIANT         491
FT                   /note="R -> K (in dbSNP:rs16979936)"
FT                   /id="VAR_054084"
FT   VARIANT         629
FT                   /note="T -> N (in dbSNP:rs6069755)"
FT                   /id="VAR_054085"
FT   VARIANT         660
FT                   /note="P -> S (in dbSNP:rs35031530)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_054086"
FT   VARIANT         780
FT                   /note="Q -> H (in dbSNP:rs7272702)"
FT                   /id="VAR_054087"
FT   CONFLICT        329
FT                   /note="Y -> N (in Ref. 1; CAC00655)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="Missing (in Ref. 1; CAC00655)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        488
FT                   /note="E -> A (in Ref. 1; CAC00655)"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..20
FT                   /evidence="ECO:0007829|PDB:2CRE"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:2CRE"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:2CRE"
FT   STRAND          51..58
FT                   /evidence="ECO:0007829|PDB:2CRE"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:2CRE"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:2CRE"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:2CRE"
SQ   SEQUENCE   786 AA;  87144 MW;  0E84CD7F60A361DB CRC64;
     MKGTGIMDCA PKALLARALY DNCPDCSDEL AFSRGDILTI LEQHVPESEG WWKCLLHGRQ
     GLAPANRLQI LTEVAADRPC PPFLRGLEEA PASSEETYQV PTLPRPPTPG PVYEQMRSWA
     EGPQPPTAQV YEFPDPPTSA RIICEKTLSF PKQAILTLPR PVRASLPTLP SQVYDVPTQH
     RGPVVLKEPE KQQLYDIPAS PKKAGLHPPD SQASGQGVPL ISVTTLRRGG YSTLPNPQKS
     EWIYDTPVSP GKASVRNTPL TSFAEESRPH ALPSSSSTFY NPPSGRSRSL TPQLNNNVPM
     QKKLSLPEIP SYGFLVPRGT FPLDEDVSYK VPSSFLIPRV EQQNTKPNIY DIPKATSSVS
     QAGKELEKAK EVSENSAGHN SSWFSRRTTS PSPEPDRLSG SSSDSRASIV SSCSTTSTDD
     SSSSSSEESA KELSLDLDVA KETVMALQHK VVSSVAGLML FVSRKWRFRD YLEANIDAIH
     RSTDHIEESV REFLDFARGV HGTACNLTDS NLQNRIRDQM QTISNSYRIL LETKESLDNR
     NWPLEVLVTD SVQNSPDDLE RFVMVARMLP EDIKRFASIV IANGRLLFKR NCEKEETVQL
     TPNAEFKCEK YIQPPQRETE SHQKSTPSTK QREDEHSSEL LKKNRANICG QNPGPLIPQP
     SSQQTPERKP RLSEHCRLYF GALFKAISAF HGSLSSSQPA EIITQSKLVI MVGQKLVDTL
     CMETQERDVR NEILRGSSHL CSLLKDVALA TKNAVLTYPS PAALGHLQAE AEKLEQHTRQ
     FRGTLG
//