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Protein N-terminal glutamine amidohydrolase (EC 3.5.1.122) (Protein NH2-terminal glutamine deamidase) (N-terminal Gln amidase) (Nt(Q)-amidase) (WDYHV motif-containing protein 1)

 NTAQ1_HUMAN             Reviewed;         205 AA.
Q96HA8; B4DE68; Q9NW95;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
25-OCT-2017, entry version 111.
RecName: Full=Protein N-terminal glutamine amidohydrolase;
EC=3.5.1.122 {ECO:0000250|UniProtKB:Q80WB5};
AltName: Full=Protein NH2-terminal glutamine deamidase;
Short=N-terminal Gln amidase;
Short=Nt(Q)-amidase;
AltName: Full=WDYHV motif-containing protein 1;
Name=WDYHV1; Synonyms=C8orf32, NTAQ1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and Embryo;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
VAL-32; SER-93; ILE-116 AND CYS-134.
TISSUE=Uterus;
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).
[5]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-205 IN COMPLEX WITH
SER-THR-ALA TRIPEPTIDE, AND SUBUNIT.
Center for eukaryotic structural genomics (CESG);
"Crystal structure of the uncharacterized human protein c8orf32 with
bound peptide.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Mediates the side-chain deamidation of N-terminal
glutamine residues to glutamate, an important step in N-end rule
pathway of protein degradation. Conversion of the resulting N-
terminal glutamine to glutamate renders the protein susceptible to
arginylation, polyubiquitination and degradation as specified by
the N-end rule. Does not act on substrates with internal or C-
terminal glutamine and does not act on non-glutamine residues in
any position. Does not deaminate acetylated N-terminal glutamine.
With the exception of proline, all tested second-position residues
on substrate peptides do not greatly influence the activity. In
contrast, a proline at position 2, virtually abolishes deamidation
of N-terminal glutamine. {ECO:0000250|UniProtKB:Q80WB5}.
-!- CATALYTIC ACTIVITY: N-terminal L-glutaminyl-[protein] + H(2)O = N-
terminal L-glutamyl-[protein] + NH(3).
{ECO:0000250|UniProtKB:Q80WB5}.
-!- SUBUNIT: Monomer. {ECO:0000269|Ref.5}.
-!- INTERACTION:
P60709:ACTB; NbExp=3; IntAct=EBI-741158, EBI-353944;
P63261:ACTG1; NbExp=5; IntAct=EBI-741158, EBI-351292;
Q4VCS5-2:AMOT; NbExp=5; IntAct=EBI-741158, EBI-3891843;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-741158, EBI-10187270;
Q96GX9:APIP; NbExp=3; IntAct=EBI-741158, EBI-359248;
P04424:ASL; NbExp=5; IntAct=EBI-741158, EBI-750131;
Q13490:BIRC2; NbExp=3; IntAct=EBI-741158, EBI-514538;
Q13867:BLMH; NbExp=3; IntAct=EBI-741158, EBI-718504;
Q9BX70:BTBD2; NbExp=4; IntAct=EBI-741158, EBI-710091;
Q9BV19:C1orf50; NbExp=5; IntAct=EBI-741158, EBI-2874661;
P20807:CAPN3; NbExp=3; IntAct=EBI-741158, EBI-5655000;
P55212:CASP6; NbExp=4; IntAct=EBI-741158, EBI-718729;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-741158, EBI-10171570;
Q52MB2:CCDC184; NbExp=3; IntAct=EBI-741158, EBI-10179526;
P32320:CDA; NbExp=5; IntAct=EBI-741158, EBI-9250559;
Q01850:CDR2; NbExp=3; IntAct=EBI-741158, EBI-1181367;
Q53EZ4:CEP55; NbExp=4; IntAct=EBI-741158, EBI-747776;
Q9Y2V7:COG6; NbExp=4; IntAct=EBI-741158, EBI-3866319;
P38432:COIL; NbExp=3; IntAct=EBI-741158, EBI-945751;
P02489:CRYAA; NbExp=5; IntAct=EBI-741158, EBI-6875961;
P32929:CTH; NbExp=3; IntAct=EBI-741158, EBI-749763;
O75553:DAB1; NbExp=3; IntAct=EBI-741158, EBI-7875264;
Q9H773:DCTPP1; NbExp=3; IntAct=EBI-741158, EBI-723569;
P49366:DHPS; NbExp=3; IntAct=EBI-741158, EBI-741925;
Q8WWZ3:EDARADD; NbExp=3; IntAct=EBI-741158, EBI-2949647;
Q14232:EIF2B1; NbExp=5; IntAct=EBI-741158, EBI-491065;
P41212:ETV6; NbExp=3; IntAct=EBI-741158, EBI-1372759;
Q6NZ44:FTH1; NbExp=3; IntAct=EBI-741158, EBI-10180219;
O60861:GAS7; NbExp=3; IntAct=EBI-741158, EBI-2683717;
O60861-1:GAS7; NbExp=4; IntAct=EBI-741158, EBI-11745923;
O60547:GMDS; NbExp=5; IntAct=EBI-741158, EBI-746373;
Q14749:GNMT; NbExp=4; IntAct=EBI-741158, EBI-744239;
Q08379:GOLGA2; NbExp=7; IntAct=EBI-741158, EBI-618309;
V9HW60:HEL-S-182mP; NbExp=3; IntAct=EBI-741158, EBI-10180762;
V9HW80:HEL-S-70; NbExp=3; IntAct=EBI-741158, EBI-10175326;
P00492:HPRT1; NbExp=8; IntAct=EBI-741158, EBI-748210;
Q9BPX1:HSD17B14; NbExp=10; IntAct=EBI-741158, EBI-742664;
P14923:JUP; NbExp=3; IntAct=EBI-741158, EBI-702484;
O95259:KCNH1; NbExp=3; IntAct=EBI-741158, EBI-2909270;
Q719H9:KCTD1; NbExp=3; IntAct=EBI-741158, EBI-9027502;
Q9H3F6:KCTD10; NbExp=4; IntAct=EBI-741158, EBI-2505886;
Q53G59:KLHL12; NbExp=7; IntAct=EBI-741158, EBI-740929;
Q15323:KRT31; NbExp=3; IntAct=EBI-741158, EBI-948001;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-741158, EBI-10172150;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-741158, EBI-10172290;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-741158, EBI-10172511;
P26371:KRTAP5-9; NbExp=5; IntAct=EBI-741158, EBI-3958099;
Q9BYQ4:KRTAP9-2; NbExp=5; IntAct=EBI-741158, EBI-1044640;
Q9BYQ2:KRTAP9-4; NbExp=3; IntAct=EBI-741158, EBI-10185730;
Q5T752:LCE1D; NbExp=4; IntAct=EBI-741158, EBI-11741311;
Q5T753:LCE1E; NbExp=4; IntAct=EBI-741158, EBI-11955335;
Q17RB8:LONRF1; NbExp=3; IntAct=EBI-741158, EBI-2341787;
Q9NQ48:LZTFL1; NbExp=3; IntAct=EBI-741158, EBI-2824799;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-741158, EBI-741037;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-741158, EBI-10178634;
P43356:MAGEA2B; NbExp=4; IntAct=EBI-741158, EBI-5650739;
Q8NA82:MARCH10; NbExp=3; IntAct=EBI-741158, EBI-2341554;
I4AY87:MIF; NbExp=3; IntAct=EBI-741158, EBI-10287234;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-741158, EBI-742948;
Q5JR59-3:MTUS2; NbExp=4; IntAct=EBI-741158, EBI-11522433;
Q9UJ70-2:NAGK; NbExp=6; IntAct=EBI-741158, EBI-11526455;
Q7Z6G3-2:NECAB2; NbExp=5; IntAct=EBI-741158, EBI-10172876;
P15531:NME1; NbExp=5; IntAct=EBI-741158, EBI-741141;
Q9BXD5:NPL; NbExp=3; IntAct=EBI-741158, EBI-10287915;
Q9BXI3:NT5C1A; NbExp=4; IntAct=EBI-741158, EBI-10441581;
O95848:NUDT14; NbExp=3; IntAct=EBI-741158, EBI-536866;
Q9P286:PAK5; NbExp=4; IntAct=EBI-741158, EBI-741896;
P61457:PCBD1; NbExp=3; IntAct=EBI-741158, EBI-740475;
Q9NXJ5-2:PGPEP1; NbExp=4; IntAct=EBI-741158, EBI-12813581;
Q8WWB5:PIH1D2; NbExp=4; IntAct=EBI-741158, EBI-10232538;
P51178:PLCD1; NbExp=4; IntAct=EBI-741158, EBI-4405387;
Q8ND90:PNMA1; NbExp=5; IntAct=EBI-741158, EBI-302345;
Q96PV4:PNMA5; NbExp=5; IntAct=EBI-741158, EBI-10171633;
Q96CD2:PPCDC; NbExp=5; IntAct=EBI-741158, EBI-724333;
Q99873:PRMT1; NbExp=3; IntAct=EBI-741158, EBI-78738;
P11908:PRPS2; NbExp=3; IntAct=EBI-741158, EBI-4290895;
Q1KLZ0:PS1TP5BP1; NbExp=3; IntAct=EBI-741158, EBI-9978131;
P61289:PSME3; NbExp=4; IntAct=EBI-741158, EBI-355546;
P11217:PYGM; NbExp=3; IntAct=EBI-741158, EBI-357469;
Q9UI14:RABAC1; NbExp=8; IntAct=EBI-741158, EBI-712367;
Q92698:RAD54L; NbExp=3; IntAct=EBI-741158, EBI-5333483;
Q93062:RBPMS; NbExp=3; IntAct=EBI-741158, EBI-740322;
Q9HAT0:ROPN1; NbExp=4; IntAct=EBI-741158, EBI-1378139;
P49247:RPIA; NbExp=6; IntAct=EBI-741158, EBI-744831;
Q9UH03:SEPT3; NbExp=3; IntAct=EBI-741158, EBI-727037;
P31947:SFN; NbExp=3; IntAct=EBI-741158, EBI-476295;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-741158, EBI-747107;
Q8NA61-2:SPERT; NbExp=4; IntAct=EBI-741158, EBI-11524851;
O75558:STX11; NbExp=3; IntAct=EBI-741158, EBI-714135;
P56279:TCL1A; NbExp=4; IntAct=EBI-741158, EBI-749995;
Q9NVV9:THAP1; NbExp=6; IntAct=EBI-741158, EBI-741515;
Q8WW34:TMEM239; NbExp=3; IntAct=EBI-741158, EBI-9675724;
A1L306:TNR; NbExp=3; IntAct=EBI-741158, EBI-10182881;
Q9H0E2:TOLLIP; NbExp=3; IntAct=EBI-741158, EBI-74615;
P14373:TRIM27; NbExp=5; IntAct=EBI-741158, EBI-719493;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-741158, EBI-2130429;
Q15645:TRIP13; NbExp=3; IntAct=EBI-741158, EBI-358993;
Q15714:TSC22D1; NbExp=3; IntAct=EBI-741158, EBI-712609;
Q15631:TSN; NbExp=4; IntAct=EBI-741158, EBI-1044160;
Q08AM6:VAC14; NbExp=3; IntAct=EBI-741158, EBI-2107455;
A5D8V6:VPS37C; NbExp=4; IntAct=EBI-741158, EBI-2559305;
P98170:XIAP; NbExp=3; IntAct=EBI-741158, EBI-517127;
Q96BR9:ZBTB8A; NbExp=3; IntAct=EBI-741158, EBI-742740;
Q9BYN7:ZNF341; NbExp=3; IntAct=EBI-741158, EBI-9089622;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q80WB5}. Nucleus
{ECO:0000250|UniProtKB:Q80WB5}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96HA8-1; Sequence=Displayed;
Name=2;
IsoId=Q96HA8-2; Sequence=VSP_055268;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the NTAQ1 family. {ECO:0000305}.
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EMBL; AK001066; BAA91488.1; -; mRNA.
EMBL; AK293492; BAG56979.1; -; mRNA.
EMBL; AC021305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471060; EAW92038.1; -; Genomic_DNA.
EMBL; BC008781; AAH08781.1; -; mRNA.
CCDS; CCDS6344.1; -. [Q96HA8-1]
CCDS; CCDS64965.1; -. [Q96HA8-2]
RefSeq; NP_001269953.1; NM_001283024.1. [Q96HA8-2]
RefSeq; NP_060494.1; NM_018024.2. [Q96HA8-1]
UniGene; Hs.18029; -.
PDB; 3C9Q; X-ray; 1.50 A; A=2-205.
PDB; 4W79; X-ray; 1.50 A; A=2-202.
PDBsum; 3C9Q; -.
PDBsum; 4W79; -.
ProteinModelPortal; Q96HA8; -.
SMR; Q96HA8; -.
BioGrid; 120405; 133.
IntAct; Q96HA8; 320.
MINT; MINT-1443224; -.
STRING; 9606.ENSP00000287387; -.
iPTMnet; Q96HA8; -.
PhosphoSitePlus; Q96HA8; -.
BioMuta; WDYHV1; -.
DMDM; 152112225; -.
EPD; Q96HA8; -.
MaxQB; Q96HA8; -.
PaxDb; Q96HA8; -.
PeptideAtlas; Q96HA8; -.
PRIDE; Q96HA8; -.
DNASU; 55093; -.
Ensembl; ENST00000287387; ENSP00000287387; ENSG00000156795. [Q96HA8-1]
Ensembl; ENST00000523984; ENSP00000430427; ENSG00000156795. [Q96HA8-2]
GeneID; 55093; -.
KEGG; hsa:55093; -.
UCSC; uc003yqn.3; human. [Q96HA8-1]
CTD; 55093; -.
EuPathDB; HostDB:ENSG00000156795.6; -.
GeneCards; WDYHV1; -.
HGNC; HGNC:25490; WDYHV1.
HPA; HPA024823; -.
HPA; HPA053680; -.
neXtProt; NX_Q96HA8; -.
OpenTargets; ENSG00000156795; -.
PharmGKB; PA164727566; -.
eggNOG; KOG3261; Eukaryota.
eggNOG; ENOG4111G3S; LUCA.
GeneTree; ENSGT00390000014398; -.
HOGENOM; HOG000007890; -.
InParanoid; Q96HA8; -.
KO; K21286; -.
OMA; NSCYCEE; -.
OrthoDB; EOG091G0K1H; -.
PhylomeDB; Q96HA8; -.
TreeFam; TF105807; -.
EvolutionaryTrace; Q96HA8; -.
GeneWiki; C8orf32; -.
GenomeRNAi; 55093; -.
PRO; PR:Q96HA8; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000156795; -.
CleanEx; HS_WDYHV1; -.
ExpressionAtlas; Q96HA8; baseline and differential.
Genevisible; Q96HA8; HS.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; ISS:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; ISS:UniProtKB.
Gene3D; 3.10.620.10; -; 1.
InterPro; IPR037132; N_Gln_amidohydro_ab_roll_sf.
InterPro; IPR023128; Prot_N_Gln_amidohydro_ab_roll.
Pfam; PF09764; Nt_Gln_amidase; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Nucleus; Polymorphism; Reference proteome.
CHAIN 1 205 Protein N-terminal glutamine
amidohydrolase.
/FTId=PRO_0000279409.
ACT_SITE 28 28 {ECO:0000250}.
ACT_SITE 81 81 {ECO:0000250}.
ACT_SITE 97 97 {ECO:0000250}.
VAR_SEQ 1 60 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055268.
VARIANT 32 32 I -> V (in dbSNP:rs6999234).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030882.
VARIANT 93 93 N -> S (in dbSNP:rs7014678).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030883.
VARIANT 116 116 F -> I (in dbSNP:rs6470147).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030884.
VARIANT 134 134 R -> C (in dbSNP:rs3824250).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030885.
HELIX 18 20 {ECO:0000244|PDB:3C9Q}.
HELIX 28 41 {ECO:0000244|PDB:3C9Q}.
STRAND 42 45 {ECO:0000244|PDB:3C9Q}.
HELIX 47 49 {ECO:0000244|PDB:3C9Q}.
STRAND 50 56 {ECO:0000244|PDB:3C9Q}.
STRAND 62 67 {ECO:0000244|PDB:3C9Q}.
STRAND 76 79 {ECO:0000244|PDB:3C9Q}.
STRAND 81 88 {ECO:0000244|PDB:3C9Q}.
TURN 89 91 {ECO:0000244|PDB:3C9Q}.
STRAND 92 96 {ECO:0000244|PDB:3C9Q}.
STRAND 100 102 {ECO:0000244|PDB:3C9Q}.
STRAND 104 107 {ECO:0000244|PDB:3C9Q}.
HELIX 108 114 {ECO:0000244|PDB:3C9Q}.
HELIX 124 126 {ECO:0000244|PDB:3C9Q}.
STRAND 129 134 {ECO:0000244|PDB:3C9Q}.
HELIX 135 141 {ECO:0000244|PDB:3C9Q}.
HELIX 147 149 {ECO:0000244|PDB:3C9Q}.
STRAND 152 154 {ECO:0000244|PDB:3C9Q}.
STRAND 156 158 {ECO:0000244|PDB:3C9Q}.
HELIX 176 179 {ECO:0000244|PDB:3C9Q}.
STRAND 185 192 {ECO:0000244|PDB:3C9Q}.
HELIX 193 200 {ECO:0000244|PDB:3C9Q}.
SEQUENCE 205 AA; 23680 MW; F858AB0C73928CA9 CRC64;
MEGNGPAAVH YQPASPPRDA CVYSSCYCEE NIWKLCEYIK NHDQYPLEEC YAVFISNERK
MIPIWKQQAR PGDGPVIWDY HVVLLHVSSG GQNFIYDLDT VLPFPCLFDT YVEDAFKSDD
DIHPQFRRKF RVIRADSYLK NFASDRSHMK DSSGNWREPP PPYPCIETGD SKMNLNDFIS
MDPKVGWGAV YTLSEFTHRF GSKNC


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