GenomeNet

Database: UniProt
Entry: Q3U962
LinkDB: Q3U962
Original site: Q3U962 
ID   CO5A2_MOUSE             Reviewed;        1497 AA.
AC   Q3U962; Q3TVR2; Q3UHK7; Q3UTT4; Q3V1J6; Q61431; Q7TMS0; Q80VS8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   18-SEP-2019, entry version 108.
DE   RecName: Full=Collagen alpha-2(V) chain;
DE   Flags: Precursor;
GN   Name=Col5a2 {ECO:0000312|MGI:MGI:88458};
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:AAA37440.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/cJ {ECO:0000312|EMBL:AAA37440.1};
RX   PubMed=1297453; DOI=10.1002/aja.1001950205;
RA   Andrikopoulos K., Suzuki H.R., Solursh M., Ramirez F.;
RT   "Localization of pro-alpha 2(V) collagen transcripts in the tissues of
RT   the developing mouse embryo.";
RL   Dev. Dyn. 195:113-120(1992).
RN   [2] {ECO:0000312|EMBL:BAE30805.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE30805.1};
RC   TISSUE=Bone marrow {ECO:0000312|EMBL:BAE30805.1},
RC   Cerebellum {ECO:0000312|EMBL:BAE23896.1},
RC   Embryo {ECO:0000312|EMBL:BAE27775.1},
RC   Placenta {ECO:0000312|EMBL:BAE27850.1}, and
RC   Skin {ECO:0000312|EMBL:BAE21154.1};
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   [3] {ECO:0000312|EMBL:AAH55077.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He {ECO:0000312|EMBL:AAH55077.1};
RC   TISSUE=Mammary gland {ECO:0000312|EMBL:AAH43696.1}, and
RC   Mesenchymal stem cell {ECO:0000312|EMBL:AAH55077.1};
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   [4] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=7704020; DOI=10.1038/ng0195-31;
RA   Andrikopoulos K., Liu X., Keene D.R., Jaenisch R., Ramirez F.;
RT   "Targeted mutation in the col5a2 gene reveals a regulatory role for
RT   type V collagen during matrix assembly.";
RL   Nat. Genet. 9:31-36(1995).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=9642685; DOI=10.1007/bf03401742;
RA   Phelps R.G., Murai C., Saito S., Hatakeyama A., Andrikopoulos K.,
RA   Kasturi K.N., Bona C.A.;
RT   "Effect of targeted mutation in collagen V alpha 2 gene on development
RT   of cutaneous hyperplasia in tight skin mice.";
RL   Mol. Med. 4:356-360(1998).
RN   [6] {ECO:0000305}
RP   SUBUNIT.
RX   PubMed=15199158; DOI=10.1128/mcb.24.13.6049-6057.2004;
RA   Chanut-Delalande H., Bonod-Bidaud C., Cogne S., Malbouyres M.,
RA   Ramirez F., Fichard A., Ruggiero F.;
RT   "Development of a functional skin matrix requires deposition of
RT   collagen V heterotrimers.";
RL   Mol. Cell. Biol. 24:6049-6057(2004).
CC   -!- FUNCTION: Type V collagen is a member of group I collagen
CC       (fibrillar forming collagen). It is a minor connective tissue
CC       component of nearly ubiquitous distribution. Type V collagen binds
CC       to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
CC       Type V collagen is a key determinant in the assembly of tissue-
CC       specific matrices. {ECO:0000250|UniProtKB:P05997,
CC       ECO:0000269|PubMed:1297453, ECO:0000269|PubMed:7704020,
CC       ECO:0000269|PubMed:9642685}.
CC   -!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains
CC       expressed in most tissues and trimers of one alpha 1(V), one alpha
CC       2(V), and one alpha 3(V) chains with a more limited distribution
CC       of expression. {ECO:0000250|UniProtKB:P05997,
CC       ECO:0000269|PubMed:15199158}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos from 9 days of gestation
CC       onward. In 12.5 dpc embryos, low and diffuse level of expression
CC       was observed in the peritoneal membranes and intestinal and
CC       craniofacial mesenchymes. By 16.5 dpc, expression is higher and
CC       exhibits a more restricted accumulation in primary ossified
CC       regions, perichondrium, joints, tendon, atrioventricular valve of
CC       heart, and in selected portions of the head.
CC       {ECO:0000269|PubMed:1297453}.
CC   -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
CC       have crucial roles in tissue growth and repair by controlling both
CC       the intracellular assembly of procollagen molecules and the
CC       extracellular assembly of collagen fibrils. It binds a calcium ion
CC       which is essential for its function (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (G-X-P) are hydroxylated in some or all of the chains.
CC       Probably 3-hydroxylated on prolines by LEPREL1.
CC   -!- PTM: Hydroxylation on proline residues within the sequence motif,
CC       GXPG, is most likely to be 4-hydroxy as this fits the requirement
CC       for 4-hydroxylation in vertebrates. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Mice homozygous for the targeted deletion of the N-
CC       terminal telopeptide segment of the COL5A2 chain show poor
CC       survival rates, possibly because of complications from spinal
CC       deformities, and exhibit skin and eye abnormalities caused by
CC       disorganized type I collagen fibrils.
CC       {ECO:0000269|PubMed:15199158, ECO:0000269|PubMed:7704020,
CC       ECO:0000269|PubMed:9642685}.
CC   -!- MISCELLANEOUS: The alpha 1(V)-alpha 1(V)-alpha 2(V) heterotrimer
CC       makes a critical contribution to fibrillogenesis, basement
CC       membrane organization, and cell viability, and may play a possible
CC       role in the development of a functional skin matrix.
CC       {ECO:0000269|PubMed:15199158}.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE23896.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; L02918; AAA37440.1; -; mRNA.
DR   EMBL; AK132413; BAE21154.1; -; mRNA.
DR   EMBL; AK139130; BAE23896.1; ALT_INIT; mRNA.
DR   EMBL; AK147220; BAE27775.1; -; mRNA.
DR   EMBL; AK147328; BAE27850.1; -; mRNA.
DR   EMBL; AK151929; BAE30805.1; -; mRNA.
DR   EMBL; AK160008; BAE35556.1; -; mRNA.
DR   EMBL; BC043696; AAH43696.1; -; mRNA.
DR   EMBL; BC055077; AAH55077.1; -; mRNA.
DR   CCDS; CCDS35555.1; -.
DR   PIR; I49607; I49607.
DR   RefSeq; NP_031763.2; NM_007737.2.
DR   SMR; Q3U962; -.
DR   ComplexPortal; CPX-2962; Collagen type V trimer variant 1.
DR   ComplexPortal; CPX-2963; Collagen type V trimer variant 2.
DR   ComplexPortal; CPX-2976; Collagen type XI trimer variant 2.
DR   ComplexPortal; CPX-2977; Collagen type XI trimer variant 3.
DR   STRING; 10090.ENSMUSP00000083620; -.
DR   iPTMnet; Q3U962; -.
DR   PhosphoSitePlus; Q3U962; -.
DR   CPTAC; non-CPTAC-4024; -.
DR   MaxQB; Q3U962; -.
DR   PaxDb; Q3U962; -.
DR   PeptideAtlas; Q3U962; -.
DR   PRIDE; Q3U962; -.
DR   Ensembl; ENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
DR   GeneID; 12832; -.
DR   KEGG; mmu:12832; -.
DR   UCSC; uc007awr.1; mouse.
DR   CTD; 1290; -.
DR   MGI; MGI:88458; Col5a2.
DR   eggNOG; KOG3544; Eukaryota.
DR   eggNOG; ENOG4110XTV; LUCA.
DR   GeneTree; ENSGT00940000155675; -.
DR   InParanoid; Q3U962; -.
DR   KO; K19721; -.
DR   OMA; LCDKIEC; -.
DR   OrthoDB; 1406711at2759; -.
DR   PhylomeDB; Q3U962; -.
DR   TreeFam; TF344135; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1474244; Extracellular matrix organization.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-186797; Signaling by PDGF.
DR   Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   Reactome; R-MMU-419037; NCAM1 interactions.
DR   Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   ChiTaRS; Col5a2; mouse.
DR   PRO; PR:Q3U962; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026042; Expressed in 303 organ(s), highest expression level in vault of skull.
DR   Genevisible; Q3U962; MM.
DR   GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR   GO; GO:0005588; C:collagen type V trimer; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0048592; P:eye morphogenesis; ISO:MGI.
DR   GO; GO:1903225; P:negative regulation of endodermal cell differentiation; ISO:MGI.
DR   GO; GO:0030903; P:notochord development; IBA:GO_Central.
DR   GO; GO:0001503; P:ossification; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001007; VWF_dom.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 6.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00214; VWC; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Collagen; Complete proteome; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27   1227       Collagen alpha-2(V) chain. {ECO:0000255}.
FT                                /FTId=PRO_0000283768.
FT   PROPEP     1228   1497       C-terminal propeptide. {ECO:0000255}.
FT                                /FTId=PRO_0000283769.
FT   DOMAIN       38     96       VWFC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN     1264   1497       Fibrillar collagen NC1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   MOTIF       141    143       Cell attachment site. {ECO:0000255}.
FT   MOTIF       504    506       Cell attachment site. {ECO:0000255}.
FT   MOTIF       942    944       Cell attachment site. {ECO:0000255}.
FT   MOTIF      1065   1067       Cell attachment site. {ECO:0000255}.
FT   MOTIF      1068   1070       Cell attachment site. {ECO:0000255}.
FT   MOTIF      1125   1127       Cell attachment site. {ECO:0000255}.
FT   MOTIF      1134   1136       Cell attachment site. {ECO:0000255}.
FT   METAL      1312   1312       Calcium. {ECO:0000250}.
FT   METAL      1314   1314       Calcium. {ECO:0000250}.
FT   METAL      1315   1315       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      1320   1320       Calcium. {ECO:0000250}.
FT   MOD_RES     288    288       4-hydroxyproline. {ECO:0000250}.
FT   MOD_RES     291    291       4-hydroxyproline. {ECO:0000250}.
FT   MOD_RES     294    294       4-hydroxyproline. {ECO:0000250}.
FT   MOD_RES     609    609       4-hydroxyproline. {ECO:0000250}.
FT   MOD_RES     615    615       4-hydroxyproline. {ECO:0000250}.
FT   CARBOHYD   1260   1260       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1398   1398       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   1294   1326       {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   DISULFID   1334   1495       {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   DISULFID   1403   1448       {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   CONFLICT     20     20       Y -> D (in Ref. 2; BAE23896).
FT                                {ECO:0000305}.
FT   CONFLICT     88     88       T -> P (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    160    160       G -> R (in Ref. 2; BAE27850).
FT                                {ECO:0000305}.
FT   CONFLICT    164    164       V -> M (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    222    222       Q -> V (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    231    231       V -> A (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    387    387       A -> R (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    390    390       T -> H (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    428    428       A -> R (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    431    431       P -> A (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    614    614       L -> V (in Ref. 1; AAA37440 and 3;
FT                                AAH55077). {ECO:0000305}.
FT   CONFLICT    666    666       Q -> A (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    809    813       PTGEK -> LLGAP (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT    851    851       P -> S (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT   1001   1002       ER -> VT (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT   1013   1013       T -> A (in Ref. 3; AAH55077).
FT                                {ECO:0000305}.
FT   CONFLICT   1063   1063       G -> V (in Ref. 2; BAE21154).
FT                                {ECO:0000305}.
FT   CONFLICT   1181   1181       P -> S (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
FT   CONFLICT   1337   1337       A -> T (in Ref. 3; AAH55077).
FT                                {ECO:0000305}.
FT   CONFLICT   1388   1388       L -> F (in Ref. 1; AAA37440).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1497 AA;  145018 MW;  CAAE15514984DB41 CRC64;
     MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR DIWKPSPCQI
     CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG GDTSFGRGRK GQKGEPGLVP
     VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP
     GPDGMSRPFS AQMAGLDEKS GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP
     GEPGPMGPIG SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR
     GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA PGKRGAHGMP
     GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG QRGETGPPGP AGSQGLPGAV
     GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK
     GEPGPHGIQG PIGPPGEEGK RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ
     GERGPVGSSG PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP
     GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP SGPVGPPGLA
     GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG AVGPLGPRGE RGNPGERGEP
     GITGLPGEKG MAGGHGPDGP KGNPGPTGTI GDTGPPGLQG MPGERGIAGT PGPKGDRGGI
     GEKGAEGTAG NDGARGLPGP LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT
     GAVGFAGPQG PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ
     GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR VGDRGPAGPP
     GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG ERGMPGLPGP AGTPGKVGPT
     GATGDKGPPG PVGPPGSNGP VGEPGPEGPA GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ
     GAPGTPGPVG APGDAGQRGE PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK
     GHRGFTGLQG LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR
     GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT EDQAAPDDTN
     KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC HPTKQSGEYW IDPNQGSAED
     AIKVYCNMET GETCISANPA SVPRKTWWAS KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT
     AITQMTFLRL LSKEASQNLT YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR
     YTVLQDTCSK RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM
//
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