GenomeNet

Database: UniProt
Entry: Q91X17
LinkDB: Q91X17
Original site: Q91X17 
ID   UROM_MOUSE              Reviewed;         642 AA.
AC   Q91X17; Q3TN64; Q3TP60; Q62285;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-FEB-2019, entry version 144.
DE   RecName: Full=Uromodulin;
DE   AltName: Full=Tamm-Horsfall urinary glycoprotein;
DE            Short=THP;
DE   Contains:
DE     RecName: Full=Uromodulin, secreted form;
DE   Flags: Precursor;
GN   Name=Umod;
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 [MRNA].
RX   PubMed=7873609; DOI=10.1016/0167-4781(94)00240-4;
RA   Prasadan K., Bates J., Badgett A., Dell M., Sukhatme V., Yu H.,
RA   Kumar S.;
RT   "Nucleotide sequence and peptide motifs of mouse uromodulin (Tamm-
RT   Horsfall protein) -- the most abundant protein in mammalian urine.";
RL   Biochim. Biophys. Acta 1260:328-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   GLYCOSYLATION, AND DOMAIN ZP.
RX   PubMed=12021773; DOI=10.1038/ncb802;
RA   Jovine L., Qi H., Williams Z., Litscher E., Wassarman P.M.;
RT   "The ZP domain is a conserved module for polymerization of
RT   extracellular proteins.";
RL   Nat. Cell Biol. 4:457-461(2002).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=14871399; DOI=10.1111/j.1523-1755.2004.00452.x;
RA   Bates J.M., Raffi H.M., Prasadan K., Mascarenhas R., Laszik Z.,
RA   Maeda N., Hultgren S.J., Kumar S.;
RT   "Tamm-Horsfall protein knockout mice are more prone to urinary tract
RT   infection: rapid communication.";
RL   Kidney Int. 65:791-797(2004).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=15327412; DOI=10.1111/j.1523-1755.2004.00867.x;
RA   Mo L., Huang H.Y., Zhu X.H., Shapiro E., Hasty D.L., Wu X.R.;
RT   "Tamm-Horsfall protein is a critical renal defense factor protecting
RT   against calcium oxalate crystal formation.";
RL   Kidney Int. 66:1159-1166(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 573-587, PROTEOLYTIC CLEAVAGE, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=18375198; DOI=10.1016/j.bbrc.2008.03.099;
RA   Santambrogio S., Cattaneo A., Bernascone I., Schwend T., Jovine L.,
RA   Bachi A., Rampoldi L.;
RT   "Urinary uromodulin carries an intact ZP domain generated by a
RT   conserved C-terminal proteolytic cleavage.";
RL   Biochem. Biophys. Res. Commun. 370:410-413(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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   [9]
RP   SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, TISSUE SPECIFICITY, AND DOMAIN.
RX   PubMed=26673890; DOI=10.7554/eLife.08887;
RA   Brunati M., Perucca S., Han L., Cattaneo A., Consolato F., Andolfo A.,
RA   Schaeffer C., Olinger E., Peng J., Santambrogio S., Perrier R., Li S.,
RA   Bokhove M., Bachi A., Hummler E., Devuyst O., Wu Q., Jovine L.,
RA   Rampoldi L.;
RT   "The serine protease hepsin mediates urinary secretion and
RT   polymerisation of Zona Pellucida domain protein uromodulin.";
RL   Elife 4:0-0(2015).
CC   -!- FUNCTION: Uromodulin: Functions in biogenesis and organization of
CC       the apical membrane of epithelial cells of the thick ascending
CC       limb of Henle's loop (TALH), where it promotes formation of
CC       complex filamentous gel-like structure that may play a role in the
CC       water barrier permeability. May serve as a receptor for binding
CC       and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates
CC       neutrophil migration across renal epithelia.
CC       {ECO:0000250|UniProtKB:P07911}.
CC   -!- FUNCTION: Uromodulin, secreted form: In the urine, may contribute
CC       to colloid osmotic pressure, retards passage of positively charged
CC       electrolytes, prevents urinary tract infection and inhibits
CC       formation of liquid containing supersaturated salts and subsequent
CC       formation of salt crystals. {ECO:0000269|PubMed:14871399,
CC       ECO:0000269|PubMed:15327412}.
CC   -!- SUBUNIT: Uromodulin, secreted form: homodimer that then
CC       polymerizes into long filaments. {ECO:0000269|PubMed:26673890}.
CC   -!- SUBCELLULAR LOCATION: Uromodulin, secreted form: Secreted
CC       {ECO:0000269|PubMed:26673890}. Note=Detected in urine.
CC       {ECO:0000269|PubMed:26673890}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:26673890}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:P07911}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:P07911}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:P07911}. Cell projection, cilium membrane
CC       {ECO:0000250|UniProtKB:P07911}. Note=Only a small fraction sorts
CC       to the basolateral pole of tubular epithelial cells compared to
CC       apical localization. Secreted into urine after cleavage.
CC       Colocalizes with NPHP1 and KIF3A. {ECO:0000250|UniProtKB:P07911}.
CC   -!- TISSUE SPECIFICITY: Detected in urine (secreted form). Detected in
CC       kidney thick ascending limb epithelial cells (at protein level).
CC       {ECO:0000269|PubMed:26673890}.
CC   -!- DOMAIN: The ZP domain mediates polymerization, leading to the
CC       formation of long filaments. {ECO:0000269|PubMed:12021773,
CC       ECO:0000269|PubMed:26673890}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12021773,
CC       ECO:0000269|PubMed:26673890}.
CC   -!- PTM: Proteolytically cleaved at a conserved C-terminal proteolytic
CC       cleavage site to generate the secreted form found in urine
CC       (PubMed:18375198). This cleavage is catalyzed by HPN
CC       (PubMed:26673890). {ECO:0000269|PubMed:18375198,
CC       ECO:0000269|PubMed:26673890}.
CC   -!- DISRUPTION PHENOTYPE: Mice suffer significantly more frequently
CC       from urinary tract infections. They shown also spontaneous
CC       formation of calcium crystals in adult kidneys, and excessive
CC       intake of calcium and oxalate dramatically increases both the
CC       frequency and the severity of renal calcium crystal formation in
CC       mutant mice, but not in wild-type mice.
CC       {ECO:0000269|PubMed:14871399, ECO:0000269|PubMed:15327412}.
DR   EMBL; L33406; AAA73896.1; -; mRNA.
DR   EMBL; AK085460; BAC39452.1; -; mRNA.
DR   EMBL; AK144065; BAE25681.1; -; mRNA.
DR   EMBL; AK164688; BAE37877.1; -; mRNA.
DR   EMBL; AK165507; BAE38225.1; -; mRNA.
DR   EMBL; BC012973; AAH12973.1; -; mRNA.
DR   CCDS; CCDS21780.1; -.
DR   PIR; S52111; S52111.
DR   RefSeq; NP_001265534.1; NM_001278605.1.
DR   RefSeq; NP_033496.1; NM_009470.5.
DR   UniGene; Mm.10826; -.
DR   ProteinModelPortal; Q91X17; -.
DR   SMR; Q91X17; -.
DR   STRING; 10090.ENSMUSP00000033263; -.
DR   iPTMnet; Q91X17; -.
DR   PhosphoSitePlus; Q91X17; -.
DR   jPOST; Q91X17; -.
DR   MaxQB; Q91X17; -.
DR   PaxDb; Q91X17; -.
DR   PRIDE; Q91X17; -.
DR   Ensembl; ENSMUST00000033263; ENSMUSP00000033263; ENSMUSG00000030963.
DR   Ensembl; ENSMUST00000209095; ENSMUSP00000146652; ENSMUSG00000030963.
DR   GeneID; 22242; -.
DR   KEGG; mmu:22242; -.
DR   UCSC; uc009jlb.2; mouse.
DR   CTD; 7369; -.
DR   MGI; MGI:102674; Umod.
DR   eggNOG; ENOG410IVSV; Eukaryota.
DR   eggNOG; ENOG410YDU6; LUCA.
DR   GeneTree; ENSGT00940000156742; -.
DR   HOGENOM; HOG000293303; -.
DR   HOVERGEN; HBG004349; -.
DR   InParanoid; Q91X17; -.
DR   KO; K18274; -.
DR   OMA; GPCGTVM; -.
DR   OrthoDB; 665331at2759; -.
DR   PhylomeDB; Q91X17; -.
DR   TreeFam; TF330284; -.
DR   Reactome; R-MMU-446203; Asparagine N-linked glycosylation.
DR   ChiTaRS; Umod; mouse.
DR   PRO; PR:Q91X17; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000030963; Expressed in 67 organ(s), highest expression level in adult mammalian kidney.
DR   ExpressionAtlas; Q91X17; baseline and differential.
DR   Genevisible; Q91X17; MM.
DR   GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019864; F:IgG binding; ISO:MGI.
DR   GO; GO:0048878; P:chemical homeostasis; IMP:MGI.
DR   GO; GO:0007588; P:excretion; IMP:MGI.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR   GO; GO:0050801; P:ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR   GO; GO:0072218; P:metanephric ascending thin limb development; IEP:UniProtKB.
DR   GO; GO:0072221; P:metanephric distal convoluted tubule development; IEP:UniProtKB.
DR   GO; GO:0072233; P:metanephric thick ascending limb development; IEP:UniProtKB.
DR   GO; GO:1990266; P:neutrophil migration; ISO:MGI.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   PRINTS; PR00023; ZPELLUCIDA.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00241; ZP; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS00682; ZP_1; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250|UniProtKB:P07911}.
FT   CHAIN        25    618       Uromodulin.
FT                                /FTId=PRO_0000041673.
FT   CHAIN        25    588       Uromodulin, secreted form.
FT                                /FTId=PRO_0000407910.
FT   PROPEP      619    642       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000041674.
FT   DOMAIN       28     64       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       65    106       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      107    148       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      335    590       ZP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00375}.
FT   REGION      431    454       Important for secretion and
FT                                polymerization into filaments.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   REGION      587    590       Essential for cleavage by HPN.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   REGION      599    608       Regulates polymerization into filaments.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   SITE        588    589       Cleavage. {ECO:0000269|PubMed:18375198,
FT                                ECO:0000269|PubMed:26673890}.
FT   LIPID       618    618       GPI-anchor amidated alanine.
FT                                {ECO:0000255}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    233    233       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    276    276       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    323    323       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    448    448       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    514    514       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     32     41       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     35     50       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     52     63       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     69     82       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     77     91       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     93    105       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    111    125       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    119    134       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    136    147       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    298    307       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    301    316       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    318    348       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    336    426       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    367    390       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    507    567       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    528    583       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    572    579       {ECO:0000250|UniProtKB:P07911}.
FT   CONFLICT     22     22       E -> G (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    102    104       ELS -> GLG (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    138    138       E -> K (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    152    152       G -> S (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    200    200       L -> Q (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    223    223       R -> A (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    255    255       Q -> H (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    279    279       A -> E (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    340    340       D -> G (in Ref. 2; BAE38225).
FT                                {ECO:0000305}.
FT   CONFLICT    473    473       H -> Y (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    590    590       S -> C (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    606    606       T -> TRQ (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    616    617       Missing (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
FT   CONFLICT    633    633       P -> L (in Ref. 1; AAA73896).
FT                                {ECO:0000305}.
SQ   SEQUENCE   642 AA;  70845 MW;  31B1461B4DCAE927 CRC64;
     MGIPLTWMLL VMMVTSWFTL AEASNSTEAR RCSECHNNAT CTVDGVVTTC SCQTGFTGDG
     LVCEDMDECA TPWTHNCSNS SCVNTPGSFK CSCQDGFRLT PELSCTDVDE CSEQGLSNCH
     ALATCVNTEG DYLCVCPEGF TGDGWYCECS PGSCEPGLDC LPQGPDGKLV CQDPCNTYET
     LTEYWRSTEY GVGYSCDAGL HGWYRFTGQG GVRMAETCVP VLRCNTAAPM WLNGSHPSSS
     EGIVSRTACA HWSDQCCRWS TEIQVKACPG GFYIYNLTAP PECNLAYCTD PSSVEGTCEE
     CRVDEDCISD NGRWRCQCKQ DSNITDVSQL EYRLECGAND IKMSLRKCQL QSLGFMNVFM
     YLNDRQCSGF SESDERDWMS IVTPARNGPC GTVLRRNETH ATYSNTLYLA NAIIIRDIII
     RMNFECSYPL DMKVSLKTSL QPMVSALNIS LGGTGKFTVR MALFQSPTYT QPHQGPSVML
     STEAFLYVGT MLDGGDLSRF VLLMTNCYAT PSSNSTDPVK YFIIQDSCPR TEDTTIQVTE
     NGESSQARFS VQMFRFAGNY DLVYLHCEVY LCDSTSEQCK PTCSGTRFRS GNFIDQTRVL
     NLGPITRQGV QASVSKAASS NLRLLSIWLL LFPSATLIFM VQ
//
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