ID   ANXA3_HUMAN             Reviewed;         323 AA.
AC   P12429; B2R9W6; Q6LET2;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Annexin A3;
DE   AltName: Full=35-alpha calcimedin;
DE   AltName: Full=Annexin III;
DE   AltName: Full=Annexin-3;
DE   AltName: Full=Inositol 1,2-cyclic phosphate 2-phosphohydrolase;
DE   AltName: Full=Lipocortin III;
DE   AltName: Full=Placental anticoagulant protein III;
DE            Short=PAP-III;
GN   Name=ANXA3; Synonyms=ANX3;
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].
RX   PubMed=2968983; DOI=10.1016/s0021-9258(18)38041-4;
RA   Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
RA   Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
RA   Hession C., Frey A.Z., Wallner B.P.;
RT   "Five distinct calcium and phospholipid binding proteins share homology
RT   with lipocortin I.";
RL   J. Biol. Chem. 263:10799-10811(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1830024; DOI=10.1016/0888-7543(91)90330-h;
RA   Tait J.F., Frankenberry D.A., Miao C.H., Killary A.M., Adler D.A.,
RA   Disteche C.M.;
RT   "Chromosomal localization of the human annexin III (ANX3) gene.";
RL   Genomics 10:441-448(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8276419; DOI=10.1006/geno.1993.1428;
RA   Tait J.F., Smith C., Xu L., Cookson B.T.;
RT   "Structure and polymorphisms of the human annexin III (ANX3) gene.";
RL   Genomics 18:79-86(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
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   [8]
RP   PROTEIN SEQUENCE OF 2-8.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [9]
RP   PROTEIN SEQUENCE OF 2-9; 40-48; 105-120; 155-163; 249-257; 264-274 AND
RP   280-288, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma;
RA   Bienvenut W.V., Heiserich L., Gottlieb E.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [10]
RP   PROTEIN SEQUENCE OF 41-102 AND 126-138.
RX   PubMed=2159184; DOI=10.1126/science.2159184;
RA   Ross T.S., Tait J.F., Majerus P.W.;
RT   "Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with
RT   lipocortin III.";
RL   Science 248:605-607(1990).
RN   [11]
RP   PROTEIN SEQUENCE OF 41-79; 85-88; 104-119; 126-150 AND 217-323.
RX   PubMed=2975506; DOI=10.1021/bi00417a011;
RA   Tait J.F., Sakata M., McMullen B.A., Miao C.H., Funakoshi T.,
RA   Hendrickson L.E., Fujikawa K.;
RT   "Placental anticoagulant proteins: isolation and comparative
RT   characterization four members of the lipocortin family.";
RL   Biochemistry 27:6268-6276(1988).
RN   [12]
RP   PROTEIN SEQUENCE OF 42-55; 74-82; 105-126; 155-169; 177-209; 264-274 AND
RP   305-315, AND CALCIUM-DEPENDENT BINDING TO PHOSPHOLIPIDS.
RX   PubMed=2138632; DOI=10.1172/jci114537;
RA   Ernst J.D., Hoye E., Blackwood R.A., Jaye D.;
RT   "Purification and characterization of an abundant cytosolic protein from
RT   human neutrophils that promotes Ca2(+)-dependent aggregation of isolated
RT   specific granules.";
RL   J. Clin. Invest. 85:1065-1071(1990).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=8639653; DOI=10.1021/bi952092o;
RA   Favier-Perron B., Lewit-Bentley A., Russo-Marie F.;
RT   "The high-resolution crystal structure of human annexin III shows subtle
RT   differences with annexin V.";
RL   Biochemistry 35:1740-1744(1996).
RN   [15]
RP   VARIANTS ASN-19; ASN-219; LEU-251 AND SER-291.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [16]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
CC   -!- FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant
CC       properties. Also cleaves the cyclic bond of inositol 1,2-cyclic
CC       phosphate to form inositol 1-phosphate.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
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DR   EMBL; M20560; AAA59496.1; -; mRNA.
DR   EMBL; M63310; AAA52284.1; -; mRNA.
DR   EMBL; L20591; AAA16713.1; -; Genomic_DNA.
DR   EMBL; CR407648; CAG28576.1; -; mRNA.
DR   EMBL; AK313945; BAG36663.1; -; mRNA.
DR   EMBL; CH471057; EAX05822.1; -; Genomic_DNA.
DR   EMBL; BC000871; AAH00871.1; -; mRNA.
DR   CCDS; CCDS3584.1; -.
DR   PIR; A47658; LUHU3.
DR   RefSeq; NP_005130.1; NM_005139.2.
DR   PDB; 1AII; X-ray; 1.95 A; A=1-323.
DR   PDB; 1AXN; X-ray; 1.78 A; A=2-323.
DR   PDBsum; 1AII; -.
DR   PDBsum; 1AXN; -.
DR   AlphaFoldDB; P12429; -.
DR   SMR; P12429; -.
DR   BioGRID; 106803; 48.
DR   IntAct; P12429; 11.
DR   MINT; P12429; -.
DR   STRING; 9606.ENSP00000264908; -.
DR   DrugBank; DB09095; Difluocortolone.
DR   DrugBank; DB03994; Ethanolamine.
DR   DrugBank; DB00591; Fluocinolone acetonide.
DR   GlyGen; P12429; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P12429; -.
DR   PhosphoSitePlus; P12429; -.
DR   SwissPalm; P12429; -.
DR   BioMuta; ANXA3; -.
DR   DMDM; 113954; -.
DR   OGP; P12429; -.
DR   CPTAC; CPTAC-17; -.
DR   CPTAC; CPTAC-18; -.
DR   EPD; P12429; -.
DR   jPOST; P12429; -.
DR   MassIVE; P12429; -.
DR   MaxQB; P12429; -.
DR   PaxDb; 9606-ENSP00000264908; -.
DR   PeptideAtlas; P12429; -.
DR   PRIDE; P12429; -.
DR   ProteomicsDB; 52852; -.
DR   Antibodypedia; 2890; 689 antibodies from 35 providers.
DR   DNASU; 306; -.
DR   Ensembl; ENST00000264908.11; ENSP00000264908.6; ENSG00000138772.13.
DR   GeneID; 306; -.
DR   KEGG; hsa:306; -.
DR   MANE-Select; ENST00000264908.11; ENSP00000264908.6; NM_005139.3; NP_005130.1.
DR   UCSC; uc003hld.4; human.
DR   AGR; HGNC:541; -.
DR   CTD; 306; -.
DR   DisGeNET; 306; -.
DR   GeneCards; ANXA3; -.
DR   HGNC; HGNC:541; ANXA3.
DR   HPA; ENSG00000138772; Tissue enhanced (bone).
DR   MIM; 106490; gene.
DR   neXtProt; NX_P12429; -.
DR   OpenTargets; ENSG00000138772; -.
DR   PharmGKB; PA24831; -.
DR   VEuPathDB; HostDB:ENSG00000138772; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000159174; -.
DR   HOGENOM; CLU_025300_0_0_1; -.
DR   InParanoid; P12429; -.
DR   OMA; KVKAIWA; -.
DR   OrthoDB; 1500773at2759; -.
DR   PhylomeDB; P12429; -.
DR   TreeFam; TF105452; -.
DR   PathwayCommons; P12429; -.
DR   SignaLink; P12429; -.
DR   SIGNOR; P12429; -.
DR   BioGRID-ORCS; 306; 17 hits in 1157 CRISPR screens.
DR   ChiTaRS; ANXA3; human.
DR   EvolutionaryTrace; P12429; -.
DR   GeneWiki; Annexin_A3; -.
DR   GenomeRNAi; 306; -.
DR   Pharos; P12429; Tbio.
DR   PRO; PR:P12429; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P12429; Protein.
DR   Bgee; ENSG00000138772; Expressed in right lung and 179 other cell types or tissues.
DR   ExpressionAtlas; P12429; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:GO_Central.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0043312; P:neutrophil degranulation; IDA:UniProtKB.
DR   GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR   GO; GO:0051054; P:positive regulation of DNA metabolic process; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR   Gene3D; 1.10.220.10; Annexin; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   InterPro; IPR002390; ANX3.
DR   PANTHER; PTHR10502; ANNEXIN; 1.
DR   PANTHER; PTHR10502:SF25; ANNEXIN A3; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00199; ANNEXINIII.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; Annexin; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
DR   SWISS-2DPAGE; P12429; -.
DR   Genevisible; P12429; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW   Direct protein sequencing; Phospholipase A2 inhibitor; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.9"
FT   CHAIN           2..323
FT                   /note="Annexin A3"
FT                   /id="PRO_0000067477"
FT   REPEAT          18..89
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          90..161
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          173..245
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          249..320
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.9"
FT   MOD_RES         267
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P14669"
FT   VARIANT         19
FT                   /note="S -> N (in dbSNP:rs5951)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013914"
FT   VARIANT         219
FT                   /note="I -> N (in dbSNP:rs5948)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013915"
FT   VARIANT         251
FT                   /note="P -> L (in dbSNP:rs5949)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013916"
FT   VARIANT         291
FT                   /note="F -> S (in dbSNP:rs5941)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013917"
FT   CONFLICT        35
FT                   /note="G -> R (in Ref. 4; CAG28576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="S -> G (in Ref. 11; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="H -> R (in Ref. 11; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           20..31
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           38..45
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           50..64
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           68..75
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           78..88
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           91..103
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           110..119
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           122..136
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           140..147
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           150..160
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           172..185
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           194..203
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           206..220
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           224..231
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           234..262
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   STRAND          263..266
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           269..279
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   TURN            280..283
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           284..295
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           299..306
FT                   /evidence="ECO:0007829|PDB:1AXN"
FT   HELIX           309..319
FT                   /evidence="ECO:0007829|PDB:1AXN"
SQ   SEQUENCE   323 AA;  36375 MW;  4128C715491FC132 CRC64;
     MASIWVGHRG TVRDYPDFSP SVDAEAIQKA IRGIGTDEKM LISILTERSN AQRQLIVKEY
     QAAYGKELKD DLKGDLSGHF EHLMVALVTP PAVFDAKQLK KSMKGAGTNE DALIEILTTR
     TSRQMKDISQ AYYTVYKKSL GDDISSETSG DFRKALLTLA DGRRDESLKV DEHLAKQDAQ
     ILYKAGENRW GTDEDKFTEI LCLRSFPQLK LTFDEYRNIS QKDIVDSIKG ELSGHFEDLL
     LAIVNCVRNT PAFLAERLHR ALKGIGTDEF TLNRIMVSRS EIDLLDIRTE FKKHYGYSLY
     SAIKSDTSGD YEITLLKICG GDD
//