GenomeNet

Database: UniProt
Entry: Q3UV74
LinkDB: Q3UV74
Original site: Q3UV74 
ID   ITB2L_MOUSE             Reviewed;         738 AA.
AC   Q3UV74; O88424; Q2KHL5;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   10-APR-2019, entry version 114.
DE   RecName: Full=Integrin beta-2-like protein;
DE   AltName: Full=Protein pactolus;
DE   Flags: Precursor;
GN   Name=Itgb2l {ECO:0000312|MGI:MGI:1277979};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC25502.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:AAC25502.1};
RC   TISSUE=Bone marrow {ECO:0000312|EMBL:AAC25502.1};
RX   PubMed=9535848; DOI=10.1074/jbc.273.15.8711;
RA   Chen Y., Garrison S., Weis J.J., Weis J.H.;
RT   "Identification of pactolus, an integrin beta subunit-like cell-
RT   surface protein preferentially expressed by cells of the bone
RT   marrow.";
RL   J. Biol. Chem. 273:8711-8718(1998).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=129/Sv {ECO:0000269|PubMed:10556426};
RX   PubMed=10556426; DOI=10.1007/s003359901164;
RA   Margraf R.L., Chen Y., Garrison S., Weis J.J., Weis J.H.;
RT   "Genomic organization, chromosomal localization, and transcriptional
RT   variants of the murine Pactolus gene.";
RL   Mamm. Genome 10:1075-1081(1999).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAE23399.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23399.1};
RC   TISSUE=Bone {ECO:0000312|EMBL:BAE23399.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAI13143.1}
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5] {ECO:0000305}
RP   SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION,
RP   POLYMORPHISM, AND VARIANT SER-539.
RX   PubMed=11461913; DOI=10.1074/jbc.M104369200;
RA   Garrison S., Hojgaard A., Patillo D., Weis J.J., Weis J.H.;
RT   "Functional characterization of pactolus, a beta-integrin-like protein
RT   preferentially expressed by neutrophils.";
RL   J. Biol. Chem. 276:35500-35511(2001).
RN   [6] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14662885; DOI=10.4049/jimmunol.171.12.6795;
RA   Garrison S., Hojgaard A., Margraf R., Weis J.J., Weis J.H.;
RT   "Surface translocation of pactolus is induced by cell activation and
RT   death, but is not required for neutrophil migration and function.";
RL   J. Immunol. 171:6795-6806(2003).
RN   [7] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16836649; DOI=10.1111/j.1365-2567.2006.02426.x;
RA   Hojgaard A., Close R., Dunn D.M., Weiss R.B., Weis J.J., Weis J.H.;
RT   "Altered localization of CXCL13 expressing cells in mice deficient in
RT   pactolus following an inflammatory stimulus.";
RL   Immunology 119:212-223(2006).
RN   [8]
RP   STRUCTURE BY NMR OF 124-335, AND SUBUNIT.
RX   PubMed=17523188; DOI=10.1002/prot.21458;
RA   Sen M., Legge G.B.;
RT   "Pactolus I-domain: functional switching of the Rossmann fold.";
RL   Proteins 68:626-635(2007).
CC   -!- FUNCTION: During inflammatory stimulation, plays a role in
CC       retaining Cxcl13-expressing cells at the site of the inflammatory
CC       response. {ECO:0000269|PubMed:16836649}.
CC   -!- SUBUNIT: Monomer and homodimer (Probable). Unlike integrin beta
CC       chains, no alpha chain partner has yet been found.
CC       {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:17523188,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11461913,
CC       ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:11461913,
CC       ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}. Note=In
CC       unactivated neutrophils, the majority of the protein is contained
CC       in intracellular granules and is released to the cell surface
CC       following inflammatory activation or induction of necrotic or
CC       apoptotic cell death. {ECO:0000269|PubMed:11461913,
CC       ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:9535848}; Synonyms=A
CC       {ECO:0000269|PubMed:10556426}, Membrane-bound
CC       {ECO:0000269|PubMed:9535848};
CC         IsoId=Q3UV74-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:9535848}; Synonyms=B
CC       {ECO:0000269|PubMed:10556426}, Truncated
CC       {ECO:0000269|PubMed:9535848};
CC         IsoId=Q3UV74-2; Sequence=VSP_052321, VSP_052322;
CC       Name=3 {ECO:0000269|PubMed:10556426}; Synonyms=C
CC       {ECO:0000269|PubMed:10556426};
CC         IsoId=Q3UV74-3; Sequence=VSP_052319, VSP_052320;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in maturing and mature
CC       neutrophils. {ECO:0000269|PubMed:11461913}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11461913}.
CC   -!- POLYMORPHISM: Strain C57BL/6 preferentially expresses isoform 1
CC       while strains BALB/c and C3H/HeJ preferentially express isoform 2.
CC       This is due to a single nucleotide difference at the second splice
CC       acceptor site in exon 13 which results in production of isoform 2
CC       when this splice site is used in strains BALB/c and C3H/HeJ.
CC       {ECO:0000269|PubMed:11461913}.
CC   -!- DISRUPTION PHENOTYPE: Mice display normal neutrophil maturation
CC       and function including appropriate migration into sites of
CC       inflammation and response to bacterial infection. Following
CC       inflammatory stimulus in the peritoneal cavity, they display
CC       decreased levels of Cxcl13 due to the migration of resident
CC       Cxcl13-expressing macrophages from the peritoneal cavity during
CC       the inflammatory response. {ECO:0000269|PubMed:14662885,
CC       ECO:0000269|PubMed:16836649}.
CC   -!- MISCELLANEOUS: The human orthologous protein seems not to exist.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000255}.
DR   EMBL; AF051367; AAC25502.1; -; mRNA.
DR   EMBL; AK137534; BAE23399.1; -; mRNA.
DR   EMBL; BC113142; AAI13143.1; -; mRNA.
DR   CCDS; CCDS28358.1; -. [Q3UV74-1]
DR   RefSeq; NP_032431.2; NM_008405.3. [Q3UV74-1]
DR   UniGene; Mm.12872; -.
DR   PDB; 2IUE; NMR; -; A=124-335.
DR   PDBsum; 2IUE; -.
DR   ProteinModelPortal; Q3UV74; -.
DR   SMR; Q3UV74; -.
DR   STRING; 10090.ENSMUSP00000000161; -.
DR   iPTMnet; Q3UV74; -.
DR   PhosphoSitePlus; Q3UV74; -.
DR   PaxDb; Q3UV74; -.
DR   PRIDE; Q3UV74; -.
DR   Ensembl; ENSMUST00000000161; ENSMUSP00000000161; ENSMUSG00000000157. [Q3UV74-1]
DR   Ensembl; ENSMUST00000131567; ENSMUSP00000114497; ENSMUSG00000000157. [Q3UV74-2]
DR   GeneID; 16415; -.
DR   KEGG; mmu:16415; -.
DR   UCSC; uc008adb.1; mouse. [Q3UV74-1]
DR   CTD; 16415; -.
DR   MGI; MGI:1277979; Itgb2l.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; Q3UV74; -.
DR   KO; K06464; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; Q3UV74; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR   Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   EvolutionaryTrace; Q3UV74; -.
DR   PRO; PR:Q3UV74; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000000157; Expressed in 44 organ(s), highest expression level in bone marrow.
DR   ExpressionAtlas; Q3UV74; baseline and differential.
DR   Genevisible; Q3UV74; MM.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IDA:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR015439; Integrin_bsu-2.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 2.
DR   PANTHER; PTHR10082:SF15; PTHR10082:SF15; 2.
DR   Pfam; PF00362; Integrin_beta; 2.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002512; Integrin_B; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SMART; SM00423; PSI; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS00243; INTEGRIN_BETA; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Inflammatory response; Integrin;
KW   Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    738       Integrin beta-2-like protein.
FT                                /FTId=PRO_0000278124.
FT   TOPO_DOM     23    671       Extracellular. {ECO:0000255}.
FT   TRANSMEM    672    692       Helical. {ECO:0000255}.
FT   TOPO_DOM    693    738       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       24     74       PSI. {ECO:0000255}.
FT   DOMAIN      126    329       VWFA. {ECO:0000255}.
FT   CARBOHYD     29     29       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    173    173       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    252    252       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    342    342       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    360    360       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    386    386       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    473    473       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    627    627       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    669    669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     25    419       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID     33     43       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID     36     73       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID     46     62       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    218    258       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    358    372       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    417    421       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    439    478       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    444    453       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    455    469       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    484    489       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    486    521       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    491    506       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    508    513       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    529    534       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    531    562       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    536    545       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    547    554       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    568    573       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    575    584       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    594    603       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    600    664       {ECO:0000250|UniProtKB:P05106}.
FT   VAR_SEQ     432    490       GGKGAMECGICRCNSGYAGKNCECQTQGPSSQDLEGSCRKD
FT                                NSSIMCSGLGDCICGQCE -> LQEDESWQPRLFSRKRPLL
FT                                LWPMLLSLQLRGLSLPVPDVHFRLSEQQDGGVQWPWSMLL
FT                                (in isoform 3).
FT                                {ECO:0000303|PubMed:10556426}.
FT                                /FTId=VSP_052319.
FT   VAR_SEQ     491    738       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10556426}.
FT                                /FTId=VSP_052320.
FT   VAR_SEQ     525    540       ERGHCSCGRCFCRYGF -> ASWAQPASAGCPLQAV (in
FT                                isoform 2). {ECO:0000303|PubMed:9535848}.
FT                                /FTId=VSP_052321.
FT   VAR_SEQ     541    738       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9535848}.
FT                                /FTId=VSP_052322.
FT   VARIANT     539    539       G -> S (in strain: BALB/c and C3H/HeJ).
FT                                {ECO:0000269|PubMed:11461913}.
FT   CONFLICT    509    509       N -> D (in Ref. 1; AAC25502 and 4;
FT                                AAI13143). {ECO:0000305}.
FT   CONFLICT    710    710       A -> V (in Ref. 1; AAC25502).
FT                                {ECO:0000305}.
FT   STRAND      127    134       {ECO:0000244|PDB:2IUE}.
FT   HELIX       137    139       {ECO:0000244|PDB:2IUE}.
FT   TURN        140    142       {ECO:0000244|PDB:2IUE}.
FT   HELIX       143    160       {ECO:0000244|PDB:2IUE}.
FT   STRAND      164    174       {ECO:0000244|PDB:2IUE}.
FT   STRAND      176    184       {ECO:0000244|PDB:2IUE}.
FT   HELIX       186    194       {ECO:0000244|PDB:2IUE}.
FT   STRAND      202    206       {ECO:0000244|PDB:2IUE}.
FT   HELIX       208    217       {ECO:0000244|PDB:2IUE}.
FT   HELIX       219    222       {ECO:0000244|PDB:2IUE}.
FT   STRAND      226    234       {ECO:0000244|PDB:2IUE}.
FT   HELIX       244    248       {ECO:0000244|PDB:2IUE}.
FT   STRAND      260    265       {ECO:0000244|PDB:2IUE}.
FT   HELIX       266    269       {ECO:0000244|PDB:2IUE}.
FT   HELIX       276    286       {ECO:0000244|PDB:2IUE}.
FT   STRAND      289    295       {ECO:0000244|PDB:2IUE}.
FT   HELIX       296    308       {ECO:0000244|PDB:2IUE}.
FT   STRAND      313    319       {ECO:0000244|PDB:2IUE}.
FT   HELIX       322    333       {ECO:0000244|PDB:2IUE}.
SQ   SEQUENCE   738 AA;  81547 MW;  CCAA3138FEFF0D5A CRC64;
     MLGQCTLLPV LAGLLSLESA LSQLCTKDNV STCQDCIRSG PSCAWCQKLN FTGRGEPDSV
     RCDTPEQLLL KGCTSEYLVD PKSLAESQED KERDQRQLSP RNVTVFLRPG QAATFKVDFQ
     RTQDNSVDLY FLMGLSGSAQ GHLSNVQTLG SDLLKALNEI SRSGRIGFGS IVNMTFQHIL
     KLTADSSQFQ RELRKQLVSG KLATPKGQLD AVVQVAICLG EIGWRNGTRF LVLVTDNDFH
     LAKDKTLGTR QNTSDGRCHL DDGMYRSRGE PDYQSVVQLA SKLAENNIQP IFVVPSRMVK
     TYEKLTTFIP KLTIGELSDD SSNVAQLIRN AYSKLSSIVV LNHSTIPSIL KVTYDSYCSN
     GTSNPGKPSG DCSGVQINDQ VTFQVNITAS ECFREQFFFI QALGFMDSVT VRVLPLCECQ
     CQEQSQHHSL CGGKGAMECG ICRCNSGYAG KNCECQTQGP SSQDLEGSCR KDNSSIMCSG
     LGDCICGQCE CHTSDIPNKE IYGQYCECNN VNCERYDGQV CGGPERGHCS CGRCFCRYGF
     VGSACQCRMS TSGCLNNRMV ECSGHGRCYC NRCLCDPGYQ PPLCEKRPGY FHRCSEYYSC
     ARCLKDNSAI KCRECWNLLF SNTPFSNKTC MTERDSEGCW TTYTLYQPDQ SDINSIYIKE
     SLVCAEISNT TILLGVIVGV LLAVIFLLVY CMVYLKGTQK AAKLPRKGGA QSTLAQQPHF
     QEPHHVEPVW NQERQGTQ
//
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