ID   RCN3_MOUSE              Reviewed;         328 AA.
AC   Q8BH97; Q58E50; Q8R137; Q99K35; Q9CTD4;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Reticulocalbin-3 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Rcn3 {ECO:0000312|MGI:MGI:1277122}; Synonyms=D7Ertd671e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Colon, 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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
RC   Testis;
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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=26252542; DOI=10.1165/rcmb.2015-0036oc;
RA   Jin J., Li Y., Ren J., Man Lam S., Zhang Y., Hou Y., Zhang X., Xu R.,
RA   Shui G., Ma R.Z.;
RT   "Neonatal Respiratory Failure with Retarded Perinatal Lung Maturation in
RT   Mice Caused by Reticulocalbin 3 Disruption.";
RL   Am. J. Respir. Cell Mol. Biol. 54:410-423(2016).
CC   -!- FUNCTION: Probable molecular chaperone assisting protein biosynthesis
CC       and transport in the endoplasmic reticulum (PubMed:26252542). Required
CC       for the proper biosynthesis and transport of pulmonary surfactant-
CC       associated protein A/SP-A, pulmonary surfactant-associated protein
CC       D/SP-D and the lipid transporter ABCA3 (PubMed:26252542). By regulating
CC       both the proper expression and the degradation through the endoplasmic
CC       reticulum-associated protein degradation pathway of these proteins
CC       plays a crucial role in pulmonary surfactant homeostasis
CC       (PubMed:26252542). Has an anti-fibrotic activity by negatively
CC       regulating the secretion of type I and type III collagens (By
CC       similarity). This calcium-binding protein also transiently associates
CC       with immature PCSK6 and regulates its secretion (By similarity).
CC       {ECO:0000250|UniProtKB:Q96D15, ECO:0000269|PubMed:26252542}.
CC   -!- SUBUNIT: Interacts with PCSK6 (immature form including the propeptide);
CC       probably involved in the maturation and the secretion of PCSK6.
CC       {ECO:0000250|UniProtKB:Q96D15}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:26252542}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung and heart. Also detected
CC       in liver, spleen, kidney, skeletal muscle, intestine, stomach, and
CC       brain. {ECO:0000269|PubMed:26252542}.
CC   -!- DEVELOPMENTAL STAGE: During lung development the expression is detected
CC       from 15.5 dpc to P1 with a maximum at 17.5 dpc which corresponds to the
CC       stage of development of alveolar saccules.
CC       {ECO:0000269|PubMed:26252542}.
CC   -!- PTM: Degraded by PCSK6 and other endoproteases including FURIN and
CC       PCSK5. {ECO:0000250|UniProtKB:Q96D15}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:I6L9G5}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous knockout mice show neonatal lethality
CC       (PubMed:26252542). Normally delivered newborn mice exhibit normal gross
CC       morphology, early motor activity, and response to painful stimuli
CC       (PubMed:26252542). They quickly develop severe respiratory distress
CC       with gasping and cyanosis, and die within 20 to 60 minutes after birth
CC       (PubMed:26252542). Normally developed trachea and diaphragm structure
CC       as well as no obvious gross morphological or histological abnormalities
CC       in the heart, brain, or liver suggest that abnormal lung development is
CC       the primary cause for the neonatal lethality (PubMed:26252542). Mutant
CC       mice exhibit morphological abnormalities of the lungs, including
CC       atelectasis with collapse of the alveolar space and unexpanded intra-
CC       alveolar septae (PubMed:26252542). This is associated with an impaired
CC       maturation of type 2 alveolar epithelial cells which is probably due to
CC       their failure to properly produce pulmonary surfactant
CC       (PubMed:26252542). {ECO:0000269|PubMed:26252542}.
CC   -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK003918; BAB23076.1; -; mRNA.
DR   EMBL; AK077943; BAC37077.1; -; mRNA.
DR   EMBL; AK082762; BAC38608.1; -; mRNA.
DR   EMBL; BC005487; AAH05487.1; -; mRNA.
DR   EMBL; BC025602; AAH25602.1; -; mRNA.
DR   EMBL; BC055903; AAH55903.1; -; mRNA.
DR   EMBL; BC092069; AAH92069.1; -; mRNA.
DR   CCDS; CCDS21229.1; -.
DR   RefSeq; NP_080831.2; NM_026555.2.
DR   RefSeq; XP_006541049.1; XM_006540986.2.
DR   RefSeq; XP_006541050.1; XM_006540987.2.
DR   AlphaFoldDB; Q8BH97; -.
DR   BioGRID; 206549; 6.
DR   IntAct; Q8BH97; 1.
DR   STRING; 10090.ENSMUSP00000019683; -.
DR   GlyConnect; 2680; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q8BH97; 1 site, 2 glycans.
DR   GlyGen; Q8BH97; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BH97; -.
DR   PhosphoSitePlus; Q8BH97; -.
DR   EPD; Q8BH97; -.
DR   jPOST; Q8BH97; -.
DR   MaxQB; Q8BH97; -.
DR   PaxDb; 10090-ENSMUSP00000019683; -.
DR   PeptideAtlas; Q8BH97; -.
DR   ProteomicsDB; 255172; -.
DR   Pumba; Q8BH97; -.
DR   Antibodypedia; 53458; 109 antibodies from 21 providers.
DR   DNASU; 52377; -.
DR   Ensembl; ENSMUST00000019683.11; ENSMUSP00000019683.4; ENSMUSG00000019539.12.
DR   Ensembl; ENSMUST00000211352.2; ENSMUSP00000148227.2; ENSMUSG00000019539.12.
DR   GeneID; 52377; -.
DR   KEGG; mmu:52377; -.
DR   UCSC; uc009gta.3; mouse.
DR   AGR; MGI:1277122; -.
DR   CTD; 57333; -.
DR   MGI; MGI:1277122; Rcn3.
DR   VEuPathDB; HostDB:ENSMUSG00000019539; -.
DR   eggNOG; KOG4223; Eukaryota.
DR   GeneTree; ENSGT01010000222360; -.
DR   HOGENOM; CLU_044718_0_1_1; -.
DR   InParanoid; Q8BH97; -.
DR   OMA; QDGKIGW; -.
DR   OrthoDB; 4490703at2759; -.
DR   PhylomeDB; Q8BH97; -.
DR   TreeFam; TF314849; -.
DR   BioGRID-ORCS; 52377; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Rcn3; mouse.
DR   PRO; PR:Q8BH97; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BH97; Protein.
DR   Bgee; ENSMUSG00000019539; Expressed in vault of skull and 212 other cell types or tissues.
DR   ExpressionAtlas; Q8BH97; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0032964; P:collagen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB.
DR   GO; GO:0060428; P:lung epithelium development; IMP:UniProtKB.
DR   GO; GO:0055091; P:phospholipid homeostasis; IMP:UniProtKB.
DR   GO; GO:0010952; P:positive regulation of peptidase activity; ISS:UniProtKB.
DR   GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR   GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI.
DR   GO; GO:0043129; P:surfactant homeostasis; IMP:UniProtKB.
DR   CDD; cd16230; EFh_CREC_RCN3; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR10827; RETICULOCALBIN; 1.
DR   PANTHER; PTHR10827:SF47; RETICULOCALBIN-3; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 6.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; Q8BH97; MM.
PE   1: Evidence at protein level;
KW   Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein; Metal-binding;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..328
FT                   /note="Reticulocalbin-3"
FT                   /id="PRO_0000004152"
FT   DOMAIN          77..112
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          113..148
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          163..198
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          200..235
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          241..276
FT                   /note="EF-hand 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          277..312
FT                   /note="EF-hand 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          24..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           325..328
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        28..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         92
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         101
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         126
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         180
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         182
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         187
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         219
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         224
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         254
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         258
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         260
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         265
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         290
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         292
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         294
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         296
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         301
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        121
FT                   /note="A -> R (in Ref. 1; BAB23076)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="R -> Q (in Ref. 2; AAH05487)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  38002 MW;  3DF05C6F0D5A6314 CRC64;
     MMWRWSFLLL LLLLRHWALG KPSPDAGPHG QDRVHHGTPL SEAPHDDAHG NFQYDHEAFL
     GRDVAKEFDK LSPEESQARL GRIVDRMDLA GDSDGWVSLA ELRAWIAHTQ QRHIRDSVSA
     AWHTYDTDRD GRVGWEELRN ATYGHYEPGE EFHDVEDAET YKKMLARDER RFRVADQDGD
     SMATREELTA FLHPEEFPHM RDIVVAETLE DLDKNKDGYV QVEEYIADLY SEEPGEEEPA
     WVQTERQQFR EFRDLNKDGR LDGSEVGYWV LPPSQDQPLV EANHLLHESD TDKDGRLSKA
     EILSNWNMFV GSQATNYGED LTRHHDEL
//