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Database: UniProt
Entry: Q61362
LinkDB: Q61362
Original site: Q61362 
ID   CH3L1_MOUSE             Reviewed;         389 AA.
AC   Q61362; B0FEU7; D3Z2P2; Q3U291; Q4FJW9; Q8BKL8; Q99J84;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 3.
DT   01-OCT-2014, entry version 122.
DE   RecName: Full=Chitinase-3-like protein 1;
DE   AltName: Full=BRP39 protein;
DE   AltName: Full=Breast regression protein 39;
DE   AltName: Full=Cartilage glycoprotein 39;
DE            Short=CGP-39;
DE            Short=GP-39;
DE   Flags: Precursor;
GN   Name=Chi3l1; Synonyms=Brp39, Chil1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=7970700;
RA   Morrison B.W., Leder P.;
RT   "neu and ras initiate murine mammary tumors that share genetic markers
RT   generally absent in c-myc and int-2-initiated tumors.";
RL   Oncogene 9:3417-3426(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF
RP   LEU-136, AND CRYSTALLIZATION.
RC   TISSUE=Mammary gland;
RX   PubMed=19041398; DOI=10.1016/j.pep.2008.11.001;
RA   Mohanty A.K., Fisher A.J., Yu Z., Pradeep M.A., Janjanam J.,
RA   Kaushik J.K.;
RT   "Cloning, expression, characterization and crystallization of BRP39, a
RT   signalling glycoprotein expressed during mammary gland apoptosis.";
RL   Protein Expr. Purif. 64:213-218(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Spinal ganglion;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16472595; DOI=10.1053/j.gastro.2005.12.007;
RA   Mizoguchi E.;
RT   "Chitinase 3-like-1 exacerbates intestinal inflammation by enhancing
RT   bacterial adhesion and invasion in colonic epithelial cells.";
RL   Gastroenterology 130:398-411(2006).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19414556; DOI=10.1084/jem.20081271;
RA   Lee C.G., Hartl D., Lee G.R., Koller B., Matsuura H., Da Silva C.A.,
RA   Sohn M.H., Cohn L., Homer R.J., Kozhich A.A., Humbles A., Kearley J.,
RA   Coyle A., Chupp G., Reed J., Flavell R.A., Elias J.A.;
RT   "Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in
RT   Th2 and IL-13-induced tissue responses and apoptosis.";
RL   J. Exp. Med. 206:1149-1166(2009).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20558631; DOI=10.1164/rccm.200912-1793OC;
RA   Sohn M.H., Kang M.J., Matsuura H., Bhandari V., Chen N.Y., Lee C.G.,
RA   Elias J.A.;
RT   "The chitinase-like proteins breast regression protein-39 and YKL-40
RT   regulate hyperoxia-induced acute lung injury.";
RL   Am. J. Respir. Crit. Care Med. 182:918-928(2010).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND REGION.
RX   PubMed=21546314; DOI=10.1016/j.clim.2011.04.007;
RA   Chen C.C., Llado V., Eurich K., Tran H.T., Mizoguchi E.;
RT   "Carbohydrate-binding motif in chitinase 3-like 1 (CHI3L1/YKL-40)
RT   specifically activates Akt signaling pathway in colonic epithelial
RT   cells.";
RL   Clin. Immunol. 140:268-275(2011).
RN   [11]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22817986; DOI=10.1016/j.chom.2012.05.017;
RA   Dela Cruz C.S., Liu W., He C.H., Jacoby A., Gornitzky A., Ma B.,
RA   Flavell R., Lee C.G., Elias J.A.;
RT   "Chitinase 3-like-1 promotes Streptococcus pneumoniae killing and
RT   augments host tolerance to lung antibacterial responses.";
RL   Cell Host Microbe 12:34-46(2012).
RN   [12]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=21866546; DOI=10.1002/ijc.26379;
RA   Libreros S., Garcia-Areas R., Shibata Y., Carrio R.,
RA   Torroella-Kouri M., Iragavarapu-Charyulu V.;
RT   "Induction of proinflammatory mediators by CHI3L1 is reduced by chitin
RT   treatment: decreased tumor metastasis in a breast cancer model.";
RL   Int. J. Cancer 131:377-386(2012).
CC   -!- FUNCTION: Carbohydrate-binding lectin with a preference for
CC       chitin. Has no chitinase activity. May play a role in tissue
CC       remodeling and in the capacity of cells to respond to and cope
CC       with changes in their environment. Plays a role in T-helper cell
CC       type 2 (Th2) inflammatory response and IL-13-induced inflammation,
CC       regulating allergen sensitization, inflammatory cell apoptosis,
CC       dendritic cell accumulation and M2 macrophage differentiation.
CC       Facilitates invasion of pathogenic enteric bacteria into colonic
CC       mucosa and lymphoid organs. Mediates activation of AKT1 signaling
CC       pathway and subsequent IL8 production in colonic epithelial cells.
CC       Regulates antibacterial responses in lung by contributing to
CC       macrophage bacterial killing, controlling bacterial dissemination
CC       and augmenting host tolerance. Also regulates hyperoxia-induced
CC       injury, inflammation and epithelial apoptosis in lung.
CC       {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19041398,
CC       ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631,
CC       ECO:0000269|PubMed:21546314, ECO:0000269|PubMed:22817986}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm.
CC       Endoplasmic reticulum. Note=Detected in bronchoalveolar lavage
CC       (BAL) fluids. Localizes mainly to endoplasmic reticulum when
CC       overexpressed in cells, with some protein also detected throughout
CC       the cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q61362-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61362-2; Sequence=VSP_054524;
CC         Note=Produced by alternative initiation at Met-9 of isoform 1.;
CC       Name=3;
CC         IsoId=Q61362-3; Sequence=VSP_054523;
CC         Note=May be produced by alternative splicing of isoform 1. Gene
CC         prediction based on EST data.;
CC   -!- TISSUE SPECIFICITY: Detected in lung in pulmonary macrophages and
CC       alveolar type 2 cells and in bronchoalveolar lavage (BAL) fluids.
CC       Expressed in mammary tumor cells (at protein level). Expressed in
CC       lung. Not detected in non-inflammatory colon.
CC       {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556,
CC       ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21866546}.
CC   -!- INDUCTION: Up-regulated in colon under several inflammatory
CC       conditions. Up-regulated upon pulmonary inflammation elicited by
CC       sensitization and challenge with the chitin-free aeroallergen
CC       ovalbumin or with chitin-containing antigen house dust mite (HDM)
CC       extract. Up-regulated in lungs after S.pneumoniae infection. Up-
CC       regulated in splenic cells of mammary tumor-bearing animals. Down-
CC       regulated by hyperoxia in lung. {ECO:0000269|PubMed:16472595,
CC       ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631,
CC       ECO:0000269|PubMed:21866546, ECO:0000269|PubMed:22817986}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and appear normal,
CC       but have defective antigen-induced Th2 inflammatory responses and
CC       defective IL-13-induced responses, displaying accelerated cell
CC       death responses and diminished M2 macrophage differentiation.
CC       Mutant mice are more sensitive to S.pneumoniae infection,
CC       displaying enhanced mortality, exacerbated lung injury and
CC       decreased bacterial clearance compared to wild-type mice. Mutant
CC       mice also have an exacerbated response to hyperoxia, displaying
CC       enhanced protein leak, tissue inflammation and chemokine
CC       production and premature death. {ECO:0000269|PubMed:19414556,
CC       ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:22817986}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family,
CC       Leu-149 is present instead of the conserved Glu which is an active
CC       site residue. Therefore this protein lacks chitinase activity.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03780.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAH04734.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAH05611.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAA63603.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR   EMBL; X93035; CAA63603.1; ALT_INIT; mRNA.
DR   EMBL; EU313768; ABY53363.1; -; mRNA.
DR   EMBL; AK051475; BAC34654.1; -; mRNA.
DR   EMBL; AK155412; BAE33251.1; -; mRNA.
DR   EMBL; CT010283; CAJ18491.1; -; mRNA.
DR   EMBL; AC137104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003780; AAH03780.1; ALT_INIT; mRNA.
DR   EMBL; BC004734; AAH04734.1; ALT_INIT; mRNA.
DR   EMBL; BC005611; AAH05611.1; ALT_INIT; mRNA.
DR   CCDS; CCDS48368.1; -. [Q61362-1]
DR   PIR; S61551; S61551.
DR   RefSeq; NP_031721.2; NM_007695.3. [Q61362-1]
DR   RefSeq; XP_006529174.1; XM_006529111.1. [Q61362-3]
DR   UniGene; Mm.38274; -.
DR   ProteinModelPortal; Q61362; -.
DR   IntAct; Q61362; 1.
DR   MINT; MINT-4090719; -.
DR   STRING; 10090.ENSMUSP00000080717; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PhosphoSite; Q61362; -.
DR   MaxQB; Q61362; -.
DR   PaxDb; Q61362; -.
DR   PRIDE; Q61362; -.
DR   Ensembl; ENSMUST00000082060; ENSMUSP00000080717; ENSMUSG00000064246. [Q61362-1]
DR   Ensembl; ENSMUST00000153856; ENSMUSP00000117117; ENSMUSG00000064246. [Q61362-2]
DR   Ensembl; ENSMUST00000156873; ENSMUSP00000119205; ENSMUSG00000064246. [Q61362-3]
DR   GeneID; 12654; -.
DR   KEGG; mmu:12654; -.
DR   UCSC; uc007crg.2; mouse. [Q61362-1]
DR   CTD; 12654; -.
DR   MGI; MGI:1340899; Chil1.
DR   eggNOG; COG3325; -.
DR   GeneTree; ENSGT00550000074323; -.
DR   HOVERGEN; HBG011684; -.
DR   InParanoid; Q4FJW9; -.
DR   KO; K17523; -.
DR   PhylomeDB; Q61362; -.
DR   TreeFam; TF315610; -.
DR   NextBio; 281872; -.
DR   PRO; PR:Q61362; -.
DR   ArrayExpress; Q61362; -.
DR   Bgee; Q61362; -.
DR   CleanEx; MM_CHI3L1; -.
DR   Genevestigator; Q61362; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
DR   GO; GO:0004568; F:chitinase activity; IEA:InterPro.
DR   GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR   GO; GO:0072606; P:interleukin-8 secretion; IDA:UniProtKB.
DR   GO; GO:0030324; P:lung development; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR   GO; GO:0070555; P:response to interleukin-1; ISS:UniProtKB.
DR   GO; GO:0070741; P:response to interleukin-6; ISS:UniProtKB.
DR   GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
DR   GO; GO:0034612; P:response to tumor necrosis factor; ISS:UniProtKB.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; -; 2.
DR   InterPro; IPR028538; CHI3L1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion.
DR   InterPro; IPR001223; Glyco_hydro18cat.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177:SF81; PTHR11177:SF81; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
DR   SUPFAM; SSF54556; SSF54556; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Alternative splicing; Antimicrobial;
KW   Apoptosis; Complete proteome; Cytoplasm; Disulfide bond;
KW   Endoplasmic reticulum; Glycoprotein; Inflammatory response;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     29       {ECO:0000250}.
FT   CHAIN        30    389       Chitinase-3-like protein 1.
FT                                /FTId=PRO_0000011966.
FT   REGION       79     80       Chitooligosaccharide binding.
FT                                {ECO:0000250}.
FT   REGION      106    109       Chitooligosaccharide binding.
FT                                {ECO:0000250}.
FT   REGION      213    216       Chitooligosaccharide binding.
FT                                {ECO:0000250}.
FT   REGION      333    347       Important for AKT1 activation and IL8
FT                                production.
FT   BINDING     150    150       Chitooligosaccharide. {ECO:0000250}.
FT   BINDING     361    361       Chitooligosaccharide. {ECO:0000250}.
FT   CARBOHYD     68     68       N-linked (GlcNAc...). {ECO:0000250}.
FT   DISULFID     34     59       {ECO:0000250}.
FT   DISULFID    309    372       {ECO:0000250}.
FT   VAR_SEQ       1     16       MHTSTEARMGMRAALT -> MTLQLA (in isoform
FT                                3). {ECO:0000305}.
FT                                /FTId=VSP_054523.
FT   VAR_SEQ       1      8       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:19041398,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_054524.
FT   MUTAGEN     136    136       L->E: No effect on chiting-binding. No
FT                                restoration of chitinase activity.
FT                                {ECO:0000269|PubMed:19041398}.
FT   CONFLICT    112    112       E -> G (in Ref. 4; ABY53363).
FT                                {ECO:0000305}.
FT   CONFLICT    258    258       A -> V (in Ref. 3; BAE33251).
FT                                {ECO:0000305}.
FT   CONFLICT    339    339       D -> H (in Ref. 1; CAA63603).
FT                                {ECO:0000305}.
FT   CONFLICT    348    348       G -> R (in Ref. 4; ABY53363).
FT                                {ECO:0000305}.
SQ   SEQUENCE   389 AA;  43893 MW;  9E7D66069B233834 CRC64;
     MHTSTEARMG MRAALTGFAV LMLLQSCSAY KLVCYFTSWS QYREGVGSFL PDAIQPFLCT
     HIIYSFANIS SDNMLSTWEW NDESNYDKLN KLKTRNTNLK TLLSVGGWKF GEKRFSEIAS
     NTERRTAFVR SVAPFLRSYG FDGLDLAWLY PRLRDKQYFS TLIKELNAEF TKEVQPGREK
     LLLSAALSAG KVAIDTGYDI AQIAQHLDFI NLMTYDFHGV WRQITGHHSP LFQGQKDTRF
     DRYSNVNYAV QYMIRLGAQA SKLLMGIPTF GKSFTLASSE NQLGAPISGE GLPGRFTKEA
     GTLAYYEICD FLKGAEVHRL SNEKVPFATK GNQWVGYEDK ESVKNKVGFL KEKKLAGAMV
     WALDLDDFQG TCQPKEFFPL TNAIKDALA
//
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