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RUN and SH3 domain-containing protein 1 (New molecule containing SH3 at the carboxy-terminus) (Nesca)

 RUSC1_HUMAN             Reviewed;         902 AA.
Q9BVN2; B3KWM9; Q5T9U9; Q5T9V0; Q5T9V1; Q5T9V2; Q9UPY4; Q9Y4T5;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
22-NOV-2017, entry version 145.
RecName: Full=RUN and SH3 domain-containing protein 1;
AltName: Full=New molecule containing SH3 at the carboxy-terminus;
Short=Nesca;
Name=RUSC1; Synonyms=NESCA;
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 2).
PubMed=10760598; DOI=10.1016/S0167-4781(00)00049-X;
Matsuda S., Miyazaki K., Ichigotani Y., Kurata H., Takenouchi Y.,
Yamamoto T., Nimura Y., Irimura T., Nakatsugawa S., Hamaguchi M.;
"Molecular cloning and characterization of a novel human gene (NESCA)
which encodes a putative adapter protein containing SH3.";
Biochim. Biophys. Acta 1491:321-326(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Lung, and Placenta;
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).
[8]
CHARACTERIZATION, AND MUTAGENESIS OF LEU-531.
PubMed=15024033; DOI=10.1083/jcb.200309081;
MacDonald J.I.S., Kubu C.J., Meakin S.O.;
"Nesca, a novel adapter, translocates to the nuclear envelope and
regulates neurotrophin-induced neurite outgrowth.";
J. Cell Biol. 164:851-862(2004).
[9]
FUNCTION, INTERACTION WITH IKBKG AND TRAF6, AND UBIQUITINATION.
PubMed=19365808; DOI=10.1002/jcp.21782;
Napolitano G., Mirra S., Monfregola J., Lavorgna A., Leonardi A.,
Ursini M.V.;
"NESCA: a new NEMO/IKKgamma and TRAF6 interacting protein.";
J. Cell. Physiol. 220:410-417(2009).
-!- FUNCTION: Putative signaling adapter which may play a role in
neuronal differentiation. May be involved in regulation of NGF-
dependent neurite outgrowth. Proposed to play a role in neuronal
vesicular trafficking, specifically involving pre-synaptic
membrane proteins. Seems to be involved in signaling pathways that
are regulated by the prolonged activation of MAPK. Can regulate
the polyubiquitination of IKBKG and thus may be involved in
regulation of the NF-kappa-B pathway.
{ECO:0000269|PubMed:19365808}.
-!- SUBUNIT: Interacts with IKBKG and TRAF6. Interacts with F-actin,
acetylated actin, TUBB3, STX1A, KIF5B and KLC1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-6257312, EBI-10175124;
Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-6257338, EBI-81279;
O60733:PLA2G6; NbExp=4; IntAct=EBI-6257312, EBI-12089905;
Q8ND90:PNMA1; NbExp=6; IntAct=EBI-6257312, EBI-302345;
Q93062:RBPMS; NbExp=3; IntAct=EBI-6257312, EBI-740322;
Q9UNE7:STUB1; NbExp=3; IntAct=EBI-6257312, EBI-357085;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-6257338, EBI-359276;
O00308:WWP2; NbExp=3; IntAct=EBI-6257312, EBI-743923;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton
{ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane,
postsynaptic density {ECO:0000250}. Golgi apparatus {ECO:0000250}.
Note=Translocated to the nuclear envelope upon stimulation with
NGF. Associated with membranes and microtubules (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9BVN2-1; Sequence=Displayed;
Name=2;
IsoId=Q9BVN2-2; Sequence=VSP_010855;
Name=3;
IsoId=Q9BVN2-3; Sequence=VSP_054052;
Name=4;
IsoId=Q9BVN2-4; Sequence=VSP_054053;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in brain.
-!- DOMAIN: The RUN domain is necessary for NGF induced nuclear
redistribution.
-!- PTM: Phosphorylated on serine residues following nuclear
translocation.
-!- PTM: Polyubiquitinated; polyubiquitination involves TRAF6.
{ECO:0000269|PubMed:19365808}.
-!- SEQUENCE CAUTION:
Sequence=AAH52277.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG54191.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB026894; BAA77507.2; -; mRNA.
EMBL; AL080083; CAB45702.1; -; mRNA.
EMBL; AK314559; BAG37144.1; -; mRNA.
EMBL; AK074982; BAG52045.1; -; mRNA.
EMBL; AK055451; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK125378; BAG54191.1; ALT_INIT; mRNA.
EMBL; BX640612; CAE45718.1; -; mRNA.
EMBL; AL139410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53069.1; -; Genomic_DNA.
EMBL; CH471121; EAW53071.1; -; Genomic_DNA.
EMBL; CH471121; EAW53072.1; -; Genomic_DNA.
EMBL; BC001045; AAH01045.1; -; mRNA.
EMBL; BC025680; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC052277; AAH52277.1; ALT_INIT; mRNA.
CCDS; CCDS1112.1; -. [Q9BVN2-2]
CCDS; CCDS41410.1; -. [Q9BVN2-1]
CCDS; CCDS41411.1; -. [Q9BVN2-4]
CCDS; CCDS41412.1; -. [Q9BVN2-3]
PIR; T12473; T12473.
RefSeq; NP_001098673.1; NM_001105203.1. [Q9BVN2-1]
RefSeq; NP_001098674.1; NM_001105204.1. [Q9BVN2-4]
RefSeq; NP_001098675.1; NM_001105205.1. [Q9BVN2-3]
RefSeq; NP_001265156.1; NM_001278227.1.
RefSeq; NP_001265157.1; NM_001278228.1.
RefSeq; NP_001265158.1; NM_001278229.1.
RefSeq; NP_001265159.1; NM_001278230.1. [Q9BVN2-2]
RefSeq; NP_055143.2; NM_014328.4. [Q9BVN2-2]
RefSeq; XP_006711320.1; XM_006711257.1. [Q9BVN2-2]
RefSeq; XP_016856381.1; XM_017000892.1.
UniGene; Hs.226499; -.
PDB; 4GIW; X-ray; 2.00 A; A/B=477-666.
PDBsum; 4GIW; -.
ProteinModelPortal; Q9BVN2; -.
SMR; Q9BVN2; -.
BioGrid; 117155; 14.
IntAct; Q9BVN2; 86.
STRING; 9606.ENSP00000357336; -.
iPTMnet; Q9BVN2; -.
PhosphoSitePlus; Q9BVN2; -.
BioMuta; RUSC1; -.
DMDM; 160380712; -.
MaxQB; Q9BVN2; -.
PaxDb; Q9BVN2; -.
PeptideAtlas; Q9BVN2; -.
PRIDE; Q9BVN2; -.
DNASU; 23623; -.
Ensembl; ENST00000292254; ENSP00000292254; ENSG00000160753. [Q9BVN2-2]
Ensembl; ENST00000368347; ENSP00000357331; ENSG00000160753. [Q9BVN2-3]
Ensembl; ENST00000368349; ENSP00000357333; ENSG00000160753. [Q9BVN2-2]
Ensembl; ENST00000368352; ENSP00000357336; ENSG00000160753. [Q9BVN2-1]
Ensembl; ENST00000368354; ENSP00000357338; ENSG00000160753. [Q9BVN2-4]
GeneID; 23623; -.
KEGG; hsa:23623; -.
UCSC; uc001fkj.3; human. [Q9BVN2-1]
CTD; 23623; -.
EuPathDB; HostDB:ENSG00000160753.15; -.
GeneCards; RUSC1; -.
H-InvDB; HIX0116321; -.
HGNC; HGNC:17153; RUSC1.
HPA; HPA028510; -.
HPA; HPA029922; -.
HPA; HPA029923; -.
MIM; 617318; gene.
neXtProt; NX_Q9BVN2; -.
OpenTargets; ENSG00000160753; -.
PharmGKB; PA134947113; -.
eggNOG; KOG0711; Eukaryota.
eggNOG; COG0142; LUCA.
GeneTree; ENSGT00900000141033; -.
HOGENOM; HOG000010280; -.
HOVERGEN; HBG058522; -.
InParanoid; Q9BVN2; -.
OMA; WKTNTGI; -.
OrthoDB; EOG091G0LEE; -.
PhylomeDB; Q9BVN2; -.
TreeFam; TF332235; -.
ChiTaRS; RUSC1; human.
GenomeRNAi; 23623; -.
PRO; PR:Q9BVN2; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160753; -.
CleanEx; HS_RUSC1; -.
ExpressionAtlas; Q9BVN2; baseline and differential.
Genevisible; Q9BVN2; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0003779; F:actin binding; ISS:UniProtKB.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
InterPro; IPR004012; Run_dom.
InterPro; IPR037213; Run_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF02759; RUN; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00593; RUN; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF140741; SSF140741; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50826; RUN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Endosome; Golgi apparatus; Membrane; Microtubule; Nucleus;
Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Reference proteome; SH3 domain; Synapse; Ubl conjugation.
CHAIN 1 902 RUN and SH3 domain-containing protein 1.
/FTId=PRO_0000097532.
DOMAIN 522 666 RUN. {ECO:0000255|PROSITE-
ProRule:PRU00178}.
DOMAIN 844 902 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 470 605 Interaction with TRAF6.
{ECO:0000269|PubMed:19365808}.
REGION 606 672 Interaction with IKBKG.
{ECO:0000269|PubMed:19365808}.
VAR_SEQ 1 469 Missing (in isoform 2).
{ECO:0000303|PubMed:10760598,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16303743,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_010855.
VAR_SEQ 1 452 MLSPQRALLCNLNHIHLQHVSLGLHLSRRPELQEGPLSTPP
PPGDTGGKESRGPCSGTLVDANSNSPAVPCRCCQEHGPGLE
NRQDPSQEEEGAASPSDPGCSSSLSSCSDLSPDESPVSVYL
RDLPGDEDAHPQPSIIPLEQGSPLASAGPGTCSPDSFCCSP
DSCSGASSSPDPGLDSNCNALTTCQDVPSPGLEEEDERAEQ
DLPTSELLEADDGKIDAGKTEPSWKINPIWKIDTEKTKAEW
KTTENNNTGWKNNGNVNSSWKSEPEKFDSGWKTNTRITDSG
SKTDAGKIDGGWRSDVSEEPVPHRTITSFHELAQKRKRGPG
LPLVPQAKKDRSDWLIVFSPDTELPPSGSPGGSSAPPREVT
TFKELRSRSRAPAPPVPPRDPPVGWALVPPRPPPPPVPPRR
KKNRPGLQPIAEGQSEEGRAVSPAAGEEAPAAKEPGAQAGL
E -> MPPTCSPGLRRQDWAPGRCAGLHLPPRAPSSPALQA
LAGQAG (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054052.
VAR_SEQ 621 726 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054053.
VARIANT 362 362 S -> F (in dbSNP:rs12061020).
/FTId=VAR_036803.
VARIANT 493 493 V -> A (in dbSNP:rs35826120).
/FTId=VAR_051329.
MUTAGEN 531 531 L->A: Abrogates nuclear redistribution.
{ECO:0000269|PubMed:15024033}.
CONFLICT 36 36 P -> S (in Ref. 7; BC025680).
{ECO:0000305}.
CONFLICT 539 539 V -> L (in Ref. 1; BAA77507).
{ECO:0000305}.
CONFLICT 770 770 P -> T (in Ref. 1; BAA77507).
{ECO:0000305}.
CONFLICT 788 788 F -> L (in Ref. 4; CAB45702).
{ECO:0000305}.
CONFLICT 793 795 GPA -> APP (in Ref. 1; BAA77507).
{ECO:0000305}.
CONFLICT 852 852 L -> F (in Ref. 4; CAB45702).
{ECO:0000305}.
CONFLICT 865 865 F -> Y (in Ref. 4; CAB45702).
{ECO:0000305}.
HELIX 484 502 {ECO:0000244|PDB:4GIW}.
HELIX 508 515 {ECO:0000244|PDB:4GIW}.
TURN 517 519 {ECO:0000244|PDB:4GIW}.
HELIX 521 529 {ECO:0000244|PDB:4GIW}.
HELIX 531 540 {ECO:0000244|PDB:4GIW}.
STRAND 545 549 {ECO:0000244|PDB:4GIW}.
TURN 550 552 {ECO:0000244|PDB:4GIW}.
STRAND 553 556 {ECO:0000244|PDB:4GIW}.
HELIX 559 566 {ECO:0000244|PDB:4GIW}.
HELIX 574 585 {ECO:0000244|PDB:4GIW}.
HELIX 592 606 {ECO:0000244|PDB:4GIW}.
HELIX 609 617 {ECO:0000244|PDB:4GIW}.
HELIX 620 626 {ECO:0000244|PDB:4GIW}.
HELIX 632 635 {ECO:0000244|PDB:4GIW}.
TURN 639 642 {ECO:0000244|PDB:4GIW}.
HELIX 643 651 {ECO:0000244|PDB:4GIW}.
HELIX 652 656 {ECO:0000244|PDB:4GIW}.
SEQUENCE 902 AA; 96444 MW; 41DB65236E766A82 CRC64;
MLSPQRALLC NLNHIHLQHV SLGLHLSRRP ELQEGPLSTP PPPGDTGGKE SRGPCSGTLV
DANSNSPAVP CRCCQEHGPG LENRQDPSQE EEGAASPSDP GCSSSLSSCS DLSPDESPVS
VYLRDLPGDE DAHPQPSIIP LEQGSPLASA GPGTCSPDSF CCSPDSCSGA SSSPDPGLDS
NCNALTTCQD VPSPGLEEED ERAEQDLPTS ELLEADDGKI DAGKTEPSWK INPIWKIDTE
KTKAEWKTTE NNNTGWKNNG NVNSSWKSEP EKFDSGWKTN TRITDSGSKT DAGKIDGGWR
SDVSEEPVPH RTITSFHELA QKRKRGPGLP LVPQAKKDRS DWLIVFSPDT ELPPSGSPGG
SSAPPREVTT FKELRSRSRA PAPPVPPRDP PVGWALVPPR PPPPPVPPRR KKNRPGLQPI
AEGQSEEGRA VSPAAGEEAP AAKEPGAQAG LEVRSSWSFA GVPGAQRLWM AEAQSGTGQL
QEQKKGLLIA VSVSVDKIIS HFGAARNLVQ KAQLGDSRLS PDVGHLVLTT LCPALHALVA
DGLKPFRKDL ITGQRRSSPW SVVEASVKPG SSTRSLGTLY SQVSRLAPLS SSRSRFHAFI
LGLLNTKQLE LWFSSLQEDA GLLSLLYLPT GFFSLARGGC PSLSTELLLL LQPLSVLTFH
LDLLFEHHHH LPLGPPQAPA PPGPPPALQQ TMQAMLHFGG RLAQSLRGTS KEAASDPSDS
PNLPTPGSWW EQLTQASRVY ASGGTEGFPL SRWAPGRHGT AAEEGAQERP LPTDEMAPGR
GLWLGRLFGV PGGPAENENG ALKSRRPSSW LPPTVSVLAL VKRGAPPEMP SPQELEASAP
RMVQTHRAVR ALCDHTAARP DQLSFRRGEV LRVITTVDED WLRCGRDGME GLVPVGYTSL
VL


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