GenomeNet

Database: UniProt
Entry: Q9CPW0
LinkDB: Q9CPW0
Original site: Q9CPW0 
ID   CNTP2_MOUSE             Reviewed;        1332 AA.
AC   Q9CPW0; Q6P2K4; Q6ZQ31;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   13-FEB-2019, entry version 145.
DE   RecName: Full=Contactin-associated protein-like 2;
DE   AltName: Full=Cell recognition molecule Caspr2;
DE   Flags: Precursor;
GN   Name=Cntnap2; Synonyms=Kiaa0868;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1332 (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCNA2, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11567047;
RA   Poliak S., Gollan L., Salomon D., Berglund E.O., Ohara R., Ranscht B.,
RA   Peles E.;
RT   "Localization of Caspr2 in myelinated nerves depends on axon-glia
RT   interactions and the generation of barriers along the axon.";
RL   J. Neurosci. 21:7568-7575(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1304 AND SER-1307, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=25378149; DOI=10.1523/JNEUROSCI.3369-14.2014;
RA   Gordon A., Adamsky K., Vainshtein A., Frechter S., Dupree J.L.,
RA   Rosenbluth J., Peles E.;
RT   "Caspr and caspr2 are required for both radial and longitudinal
RT   organization of myelinated axons.";
RL   J. Neurosci. 34:14820-14826(2014).
CC   -!- FUNCTION: Required, with CNTNAP1, for radial and longitudinal
CC       organization of myelinated axons (PubMed:25378149). Plays a role
CC       in the formation of functional distinct domains critical for
CC       saltatory conduction of nerve impulses in myelinated nerve fibers.
CC       Demarcates the juxtaparanodal region of the axo-glial junction
CC       (Probable) (PubMed:25378149). {ECO:0000269|PubMed:25378149,
CC       ECO:0000305|PubMed:11567047}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with KCNA2.
CC       {ECO:0000269|PubMed:11567047}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11567047};
CC       Single-pass type I membrane protein {ECO:0000305}. Cell
CC       projection, axon {ECO:0000269|PubMed:11567047,
CC       ECO:0000269|PubMed:25378149}. Cell junction, paranodal septate
CC       junction {ECO:0000269|PubMed:25378149}. Note=Expressed in the
CC       juxtaparadonal region. {ECO:0000269|PubMed:25378149}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CPW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CPW0-2; Sequence=VSP_014977;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: In sciatic nerve predominantly found at the
CC       juxtaparanodal regions (at protein level).
CC       {ECO:0000269|PubMed:11567047, ECO:0000269|PubMed:25378149}.
CC   -!- DEVELOPMENTAL STAGE: Detected at postnatal day 8 in sciatic nerve
CC       at the paranodes and the juxtaparanodal region. Is progressively
CC       translocated to the adjacent juxtaparanodal region until it
CC       becomes completely absent from the paranodes in the adult.
CC       {ECO:0000269|PubMed:11567047}.
CC   -!- DISRUPTION PHENOTYPE: Mutants don't show difference of Ranvier
CC       nodes length and width compared to wild-type littermates. Double
CC       mutants CNTNAP1 and CNTNAP2 have wider Ranvier nodes.
CC       {ECO:0000269|PubMed:25378149}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98042.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AK017341; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK013139; BAB28674.1; -; mRNA.
DR   EMBL; AK129232; BAC98042.1; ALT_INIT; mRNA.
DR   EMBL; BC029826; AAH29826.1; -; mRNA.
DR   EMBL; BC064467; AAH64467.1; -; mRNA.
DR   CCDS; CCDS20094.1; -. [Q9CPW0-2]
DR   CCDS; CCDS39475.1; -. [Q9CPW0-1]
DR   RefSeq; NP_001004357.2; NM_001004357.2.
DR   RefSeq; NP_080047.1; NM_025771.3. [Q9CPW0-2]
DR   UniGene; Mm.440084; -.
DR   ProteinModelPortal; Q9CPW0; -.
DR   SMR; Q9CPW0; -.
DR   CORUM; Q9CPW0; -.
DR   STRING; 10090.ENSMUSP00000110288; -.
DR   iPTMnet; Q9CPW0; -.
DR   PhosphoSitePlus; Q9CPW0; -.
DR   PaxDb; Q9CPW0; -.
DR   PeptideAtlas; Q9CPW0; -.
DR   PRIDE; Q9CPW0; -.
DR   Ensembl; ENSMUST00000060839; ENSMUSP00000056299; ENSMUSG00000039419. [Q9CPW0-2]
DR   Ensembl; ENSMUST00000199100; ENSMUSP00000143528; ENSMUSG00000039419. [Q9CPW0-2]
DR   GeneID; 66797; -.
DR   KEGG; mmu:66797; -.
DR   CTD; 26047; -.
DR   MGI; MGI:1914047; Cntnap2.
DR   eggNOG; KOG3516; Eukaryota.
DR   eggNOG; ENOG410XPHG; LUCA.
DR   GeneTree; ENSGT00940000154516; -.
DR   HOGENOM; HOG000230964; -.
DR   HOVERGEN; HBG057718; -.
DR   InParanoid; Q9CPW0; -.
DR   KO; K07380; -.
DR   OrthoDB; 338397at2759; -.
DR   PhylomeDB; Q9CPW0; -.
DR   ChiTaRS; Cntnap2; mouse.
DR   PRO; PR:Q9CPW0; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000039419; Expressed in 189 organ(s), highest expression level in olfactory bulb.
DR   ExpressionAtlas; Q9CPW0; baseline and differential.
DR   Genevisible; Q9CPW0; MM.
DR   GO; GO:0030673; C:axolemma; ISS:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISS:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0033270; C:paranode region of axon; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
DR   GO; GO:0044325; F:ion channel binding; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0030534; P:adult behavior; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; TAS:BHF-UCL.
DR   GO; GO:0045163; P:clustering of voltage-gated potassium channels; IMP:BHF-UCL.
DR   GO; GO:0007612; P:learning; ISO:MGI.
DR   GO; GO:0021761; P:limbic system development; IEP:BHF-UCL.
DR   GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR   GO; GO:0008038; P:neuron recognition; TAS:BHF-UCL.
DR   GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:UniProtKB.
DR   GO; GO:0035176; P:social behavior; ISO:MGI.
DR   GO; GO:0042297; P:vocal learning; ISO:MGI.
DR   GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR   CDD; cd00057; FA58C; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR029831; Caspr2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR003585; Neurexin-like.
DR   PANTHER; PTHR43925:SF3; PTHR43925:SF3; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 4.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell junction; Cell projection;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   1332       Contactin-associated protein-like 2.
FT                                /FTId=PRO_0000019507.
FT   TOPO_DOM     28   1262       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1263   1283       Helical. {ECO:0000255}.
FT   TOPO_DOM   1284   1332       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       35    181       F5/8 type C. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN      187    368       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      373    552       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      554    591       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      592    798       Fibrinogen C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   DOMAIN      799    963       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      964   1002       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1023   1214       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   MOD_RES    1304   1304       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1307   1307       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    289    289       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    346    346       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    379    379       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    436    436       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    507    507       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    546    546       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    630    630       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    735    735       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1117   1117       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1199   1199       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     35    181       {ECO:0000250}.
FT   DISULFID    336    368       {ECO:0000250}.
FT   DISULFID    520    552       {ECO:0000250}.
FT   DISULFID    558    569       {ECO:0000250}.
FT   DISULFID    563    578       {ECO:0000250}.
FT   DISULFID    580    590       {ECO:0000250}.
FT   DISULFID    936    963       {ECO:0000250}.
FT   DISULFID    967    980       {ECO:0000250}.
FT   DISULFID    974    989       {ECO:0000250}.
FT   DISULFID    991   1001       {ECO:0000250}.
FT   DISULFID   1179   1215       {ECO:0000250}.
FT   VAR_SEQ       1   1224       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_014977.
FT   CONFLICT    357    357       G -> E (in Ref. 3; AAH64467).
FT                                {ECO:0000305}.
FT   CONFLICT    538    538       Q -> H (in Ref. 3; AAH64467).
FT                                {ECO:0000305}.
FT   CONFLICT   1192   1192       K -> N (in Ref. 3; AAH64467).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1332 AA;  148197 MW;  6AA097C69D83F0A5 CRC64;
     MVMSLRAGYR AALSLWILSS FICRAWTAPS TFQKCDEPLI SGLPHVSFSS SSSLSSSYAP
     GYAKINKRGG AGGWSPSDSD HYQWLQVDFG NRKQISAIAT QGRYSSSDWV TQYRMLYSDT
     GRNWKPYHQD GNIWAFPGNI NSDSVVRHDL QHAVVARYVR IVPLDWNGEG HIGLRAEVYG
     CAYWADVINF DGHGVLPYRF RNKKMKTLKD VIALKFKTSE SEGVLLHGEG QQGDYITLEL
     KKAKLVLSLN LGSNQLGPIY GHTSVTSGSL LDDHHWHSVL IERQGRSINL TLDRSMQHFR
     TNGEFDYLDL DYEITFGGIP FSGKPSSSNR KNFKGCMESI NYNGVNITDL ARRKKLGPSN
     MGNLSFSCVE PYTVPVFFNA TSYLEVPGRL NQDLFSVSFQ FRTWNPSGLL LFSHFADNLG
     NVEIDLVESK VGVHINNTQT KTSQIDISSG SGLNDGQWHE VRFLAKENFA VLTIDGDEAS
     AVRTNSPLQV KTGEKYFFGG FLNHMNNASY SALQPSFQGC MQLIQVDDQL VNLYEVAQRK
     PGSFANVTID MCAIIDRCVP NHCEHGGKCS QTWDSFKCTC DETGYSGATC HNSIYEPSCE
     AYKHLGQTSN YYWIDPDGSG PLGPLKVYCN MTEDKVWTIV SHDLQMQTTV VGYNPEKYSV
     TQLIYSASMD QISAITSSAE YCEQYVSYFC RMSRLLNTPD GSPYTWWVGK ANEKHYYWGG
     SEPGIQKCAC GIERNCTDPK YYCNCDADYK QWRKDAGFLS YKDHLPVSQV VVGDTDRQGS
     EAKLSVGPLR CQGDRNYWNA ASFPNPSSYL HFSTFQGETS ADISFYFKTL IPRGVFLENL
     GNTDFIKLEL KSATEVSFSF DVGNGPVEIV VRSPSPLNDD QWHRVTAERN VKQASLQVDR
     LPQQIRKAPT EGHTRLELYS QLFVGGAGGQ QGFLGCIRSL RMNGVTLDLE ERAKVTSGFK
     SGCSGHCTSY GANCENGGKC IEKYHGYSCD CSNTAYDGTF CNKDVGAFFE EGMWLRYNFQ
     APAVTARDTG SRAENSADQQ QHLAPDLAQE QIHFSFSTTK APCILLYVSS LTTDFLAVLV
     KPTGNLQIRY NLGGTREPFN IDVDHRNMAN GQPHSVNITR HERTIILKLD HYPAVGYHLP
     SSSDTLFNSP KSLFLGKVIE TGKIDQEIHK YNTPGFTGCL SRVQFNHIAP LKAALRQTNA
     SAHVHIQGEL VESNCGASPL TLSPMSSATD PWHLDHLDSA SADFPYNPGQ GQAIRNGVNR
     NSAIIGGVIA VVIFTILCTL VFLIRYMFRH KGTYHTNEAK GAESAESADA AIMNNDPNFT
     ETIDESKKEW LI
//
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