ID   NECA3_HUMAN             Reviewed;         396 AA.
AC   Q96P71; A8K780; E1P5N2; Q5JWF5; Q5JWF6; Q5JWF7; Q86VV1; Q9H433; Q9H8G8;
AC   Q9HBW7; Q9HCQ9;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=N-terminal EF-hand calcium-binding protein 3;
DE   AltName: Full=Amyloid-beta A4 protein-binding family A member 2-binding protein;
DE   AltName: Full=Nek2-interacting protein 1;
DE   AltName: Full=Neuronal calcium-binding protein 3;
DE   AltName: Full=X11L-binding protein 51;
GN   Name=NECAB3; Synonyms=APBA2BP, NIP1, SYTIP2, XB51;
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), AND TISSUE SPECIFICITY.
RX   PubMed=12044471; DOI=10.1016/s0306-4522(02)00063-5;
RA   Sugita S., Ho A., Suedhof T.C.;
RT   "NECABs: a family of neuronal Ca(2+)-binding proteins with an unusual
RT   domain structure and a restricted expression pattern.";
RL   Neuroscience 112:51-63(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NEK2, SUBCELLULAR
RP   LOCATION, AND PHOSPHORYLATION.
RC   TISSUE=Liver;
RX   PubMed=14697346; DOI=10.1016/j.yexcr.2003.09.025;
RA   Yoo J.C., Chang J.R., Kim S.H., Jang S.K., Wolgemuth D.J., Kim K., Rhee K.;
RT   "NIP1/XB51/NECAB3 is a potential substrate of Nek2, suggesting specific
RT   roles of Nek2 in Golgi.";
RL   Exp. Cell Res. 292:393-402(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Placenta, and Skeletal muscle;
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 65-396 (ISOFORM 2), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH APBA2.
RC   TISSUE=Brain;
RX   PubMed=10833507; DOI=10.1074/jbc.c000302200;
RA   Lee D.-S., Tomita S., Kirino Y., Suzuki T.;
RT   "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51,
RT   a novel X11L-binding protein.";
RL   J. Biol. Chem. 275:23134-23138(2000).
RN   [8]
RP   FUNCTION, INTERACTION WITH APBA3 AND HIF1AN, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF HIS-358.
RX   PubMed=26948053; DOI=10.1038/srep22784;
RA   Nakaoka H.J., Hara T., Yoshino S., Kanamori A., Matsui Y., Shimamura T.,
RA   Sato H., Murakami Y., Seiki M., Sakamoto T.;
RT   "NECAB3 promotes activation of hypoxia-inducible factor-1 during normoxia
RT   and enhances tumourigenicity of cancer cells.";
RL   Sci. Rep. 6:22784-22784(2016).
CC   -!- FUNCTION: Inhibits the interaction of APBA2 with amyloid-beta precursor
CC       protein (APP), and hence allows formation of amyloid-beta. May enhance
CC       the activity of HIF1A and thus promote glycolysis under normoxic
CC       conditions; the function requires its ABM domain and may implicate the
CC       stabilization of the interaction between HIF1AN and APBA3.
CC       {ECO:0000269|PubMed:10833507, ECO:0000269|PubMed:26948053}.
CC   -!- SUBUNIT: Interacts with the N-terminal domain of APBA2. Interacts with
CC       NEK2. Interacts with APBA3; APBA3 seems to mediate the interaction
CC       between NECAB3 and HIF1AN. {ECO:0000269|PubMed:10833507,
CC       ECO:0000269|PubMed:14697346, ECO:0000269|PubMed:26948053}.
CC   -!- INTERACTION:
CC       Q96P71; O96018: APBA3; NbExp=2; IntAct=EBI-5773009, EBI-6115839;
CC       Q96P71-2; O96018: APBA3; NbExp=4; IntAct=EBI-15098952, EBI-6115839;
CC       Q96P71-2; P21917: DRD4; NbExp=3; IntAct=EBI-15098952, EBI-8592297;
CC       Q96P71-2; Q14114-3: LRP8; NbExp=3; IntAct=EBI-15098952, EBI-25832196;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10833507,
CC       ECO:0000269|PubMed:14697346, ECO:0000269|PubMed:26948053}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist. Experimental confirmation
CC         may be lacking for some isoforms.;
CC       Name=2; Synonyms=XB51-alpha;
CC         IsoId=Q96P71-1; Sequence=Displayed;
CC       Name=1; Synonyms=XB51-beta;
CC         IsoId=Q96P71-2; Sequence=VSP_000739;
CC       Name=3;
CC         IsoId=Q96P71-3; Sequence=VSP_000737, VSP_000738;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle,
CC       moderately in brain and pancreas. {ECO:0000269|PubMed:10833507,
CC       ECO:0000269|PubMed:12044471}.
CC   -!- PTM: Phosphorylated by NEK2. {ECO:0000305|PubMed:14697346}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May result from the retention of an intron
CC       in the cDNA. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14649.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB16413.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF193759; AAG28415.1; -; mRNA.
DR   EMBL; AF409141; AAL01118.1; -; mRNA.
DR   EMBL; AK023706; BAB14649.1; ALT_FRAME; mRNA.
DR   EMBL; AK291895; BAF84584.1; -; mRNA.
DR   EMBL; AL121906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76302.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76304.1; -; Genomic_DNA.
DR   EMBL; BC047673; AAH47673.1; -; mRNA.
DR   EMBL; AB039947; BAB16413.1; ALT_INIT; mRNA.
DR   CCDS; CCDS42866.1; -. [Q96P71-1]
DR   CCDS; CCDS42867.1; -. [Q96P71-2]
DR   RefSeq; NP_112508.3; NM_031231.3. [Q96P71-2]
DR   RefSeq; NP_112509.3; NM_031232.3. [Q96P71-1]
DR   AlphaFoldDB; Q96P71; -.
DR   SMR; Q96P71; -.
DR   BioGRID; 122006; 10.
DR   CORUM; Q96P71; -.
DR   IntAct; Q96P71; 11.
DR   MINT; Q96P71; -.
DR   STRING; 9606.ENSP00000246190; -.
DR   CarbonylDB; Q96P71; -.
DR   iPTMnet; Q96P71; -.
DR   PhosphoSitePlus; Q96P71; -.
DR   BioMuta; NECAB3; -.
DR   DMDM; 41688800; -.
DR   jPOST; Q96P71; -.
DR   MassIVE; Q96P71; -.
DR   PaxDb; 9606-ENSP00000246190; -.
DR   PeptideAtlas; Q96P71; -.
DR   ProteomicsDB; 77645; -. [Q96P71-1]
DR   ProteomicsDB; 77646; -. [Q96P71-2]
DR   ProteomicsDB; 77647; -. [Q96P71-3]
DR   Pumba; Q96P71; -.
DR   Antibodypedia; 25664; 168 antibodies from 26 providers.
DR   DNASU; 63941; -.
DR   Ensembl; ENST00000246190.11; ENSP00000246190.6; ENSG00000125967.17. [Q96P71-1]
DR   Ensembl; ENST00000375238.8; ENSP00000364386.4; ENSG00000125967.17. [Q96P71-2]
DR   GeneID; 63941; -.
DR   KEGG; hsa:63941; -.
DR   MANE-Select; ENST00000246190.11; ENSP00000246190.6; NM_031232.4; NP_112509.3.
DR   UCSC; uc002wzm.5; human. [Q96P71-1]
DR   AGR; HGNC:15851; -.
DR   CTD; 63941; -.
DR   DisGeNET; 63941; -.
DR   GeneCards; NECAB3; -.
DR   HGNC; HGNC:15851; NECAB3.
DR   HPA; ENSG00000125967; Low tissue specificity.
DR   MIM; 612478; gene.
DR   neXtProt; NX_Q96P71; -.
DR   OpenTargets; ENSG00000125967; -.
DR   PharmGKB; PA24871; -.
DR   VEuPathDB; HostDB:ENSG00000125967; -.
DR   eggNOG; ENOG502QWRY; Eukaryota.
DR   GeneTree; ENSGT00950000183131; -.
DR   InParanoid; Q96P71; -.
DR   OMA; IDKLECQ; -.
DR   OrthoDB; 2900383at2759; -.
DR   PhylomeDB; Q96P71; -.
DR   TreeFam; TF331029; -.
DR   PathwayCommons; Q96P71; -.
DR   SignaLink; Q96P71; -.
DR   BioGRID-ORCS; 63941; 16 hits in 1158 CRISPR screens.
DR   ChiTaRS; NECAB3; human.
DR   GeneWiki; APBA2BP; -.
DR   GenomeRNAi; 63941; -.
DR   Pharos; Q96P71; Tbio.
DR   PRO; PR:Q96P71; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q96P71; Protein.
DR   Bgee; ENSG00000125967; Expressed in right adrenal gland cortex and 194 other cell types or tissues.
DR   ExpressionAtlas; Q96P71; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000137; C:Golgi cis cisterna; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019538; P:protein metabolic process; IDA:UniProtKB.
DR   GO; GO:0009306; P:protein secretion; NAS:UniProtKB.
DR   GO; GO:0042984; P:regulation of amyloid precursor protein biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR039862; NECAB1/2/3.
DR   PANTHER; PTHR12178; EF-HAND DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12178:SF3; N-TERMINAL EF-HAND CALCIUM-BINDING PROTEIN 3; 1.
DR   Pfam; PF03992; ABM; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   SMART; SM00054; EFh; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS51725; ABM; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   Genevisible; Q96P71; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Golgi apparatus; Metal-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..396
FT                   /note="N-terminal EF-hand calcium-binding protein 3"
FT                   /id="PRO_0000073863"
FT   DOMAIN          36..71
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          296..385
FT                   /note="ABM"
FT   REGION          14..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..190
FT                   /note="Required for interaction with APBA3"
FT                   /evidence="ECO:0000269|PubMed:26948053"
FT   REGION          197..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   VAR_SEQ         176..203
FT                   /note="SDAESVEAQSRLCGSRRAGRRALRSVSR -> YVRVLSTCGASAQAPIVPPF
FT                   QIPTVPAS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_000737"
FT   VAR_SEQ         204..396
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_000738"
FT   VAR_SEQ         242..275
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:12044471,
FT                   ECO:0000303|PubMed:14697346, ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_000739"
FT   VARIANT         254
FT                   /note="P -> L (in dbSNP:rs17124890)"
FT                   /id="VAR_048643"
FT   MUTAGEN         358
FT                   /note="H->A: No effect on interaction with APBA3."
FT                   /evidence="ECO:0000269|PubMed:26948053"
FT   CONFLICT        383
FT                   /note="T -> I (in Ref. 1; AAG28415)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  44350 MW;  9B24503AA629CB45 CRC64;
     MACAGLLTVC LLRPPAPQPQ PQTPRHPQLA PDPGPAGHTL FQDVFRRADK NDDGKLSFEE
     FQNYFADGVL SLGELQELFS GIDGHLTDNL ETEKLCDYFS EHLGVYRPVL AALESLNRAV
     LAAMDATKLE YERASKVDQF VTRFLLRETV SQLQALQSSL EGASDTLEAQ AHGWRSDAES
     VEAQSRLCGS RRAGRRALRS VSRSSTWSPG SSDTGRSSEA EMQWRLQVNR LQELIDQLEC
     KVRAVGPGPH KGGPSWYPPE PGPCWRPGPH SVPSQAPRLE PLREEDLAKG PDLHILMAQR
     QVQVAEEGLQ DFHRALRCYV DFTGAQSHCL HVSAQKMLDG ASFTLYEFWQ DEASWRRHQQ
     SPGSKAFQRI LIDHLRAPDT LTTVFFPASW WIMNNN
//