UROM_MOUSE
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 03-AUG-2022, entry version 162.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Kumar S.;
RT "Nucleotide sequence and peptide motifs of mouse uromodulin (Tamm-Horsfall
RT 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., 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 [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 project:
RT 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 extracellular
RT 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., Maeda N.,
RA 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 BY
RP 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 conserved C-
RT 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 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 polymerisation
RT of Zona Pellucida domain protein uromodulin.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: [Uromodulin]: Functions in biogenesis and organization of the
CC apical membrane of epithelial cells of the thick ascending limb of
CC Henle's loop (TALH), where it promotes formation of complex filamentous
CC gel-like structure that may play a role in the water barrier
CC permeability. May serve as a receptor for binding and endocytosis of
CC cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across
CC renal epithelia. {ECO:0000250|UniProtKB:P07911}.
CC -!- FUNCTION: [Uromodulin, secreted form]: In the urine, may contribute to
CC colloid osmotic pressure, retards passage of positively charged
CC electrolytes, prevents urinary tract infection and inhibits formation
CC of liquid containing supersaturated salts and subsequent formation of
CC salt crystals. {ECO:0000269|PubMed:14871399,
CC ECO:0000269|PubMed:15327412}.
CC -!- SUBUNIT: [Uromodulin, secreted form]: Homodimer that then polymerizes
CC into long filaments (PubMed:26673890). The filaments can additionally
CC assemble laterally to form a sheet (By similarity).
CC {ECO:0000250|UniProtKB:P07911, 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 to the
CC basolateral pole of tubular epithelial cells compared to apical
CC localization. Secreted into urine after cleavage. Colocalizes with
CC 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 formation
CC of long filaments (PubMed:12021773, PubMed:26673890). The core of the
CC filament consists of stacked ZP domains which assemble into a helical
CC structure. Each ZP domain consists of an N-terminal (ZP-N) and C-
CC terminal (ZP-C) region connected by a flexible linker; the linker
CC allows the ZP domain to wrap around the ZP-C subdomain of the preceding
CC subunit. The heavily glycosylated N-terminal part of the protein
CC (containing several EGF-like domains) forms branches which protrude
CC from the core and may be involved in pathogen capture (By similarity).
CC {ECO:0000250|UniProtKB:P07911, 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 (PubMed:26673890).
CC {ECO:0000269|PubMed:18375198, ECO:0000269|PubMed:26673890}.
CC -!- DISRUPTION PHENOTYPE: Mice suffer significantly more frequently from
CC urinary tract infections. They shown also spontaneous formation of
CC calcium crystals in adult kidneys, and excessive intake of calcium and
CC oxalate dramatically increases both the frequency and the severity of
CC renal calcium crystal formation in mutant mice, but not in wild-type
CC mice. {ECO:0000269|PubMed:14871399, ECO:0000269|PubMed:15327412}.
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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 AlphaFoldDB; Q91X17; -.
DR SMR; Q91X17; -.
DR IntAct; Q91X17; 1.
DR MINT; Q91X17; -.
DR STRING; 10090.ENSMUSP00000033263; -.
DR GlyGen; Q91X17; 10 sites.
DR iPTMnet; Q91X17; -.
DR PhosphoSitePlus; Q91X17; -.
DR CPTAC; non-CPTAC-3626; -.
DR jPOST; Q91X17; -.
DR MaxQB; Q91X17; -.
DR PaxDb; Q91X17; -.
DR PRIDE; Q91X17; -.
DR ProteomicsDB; 297899; -.
DR Antibodypedia; 4003; 568 antibodies from 38 providers.
DR DNASU; 22242; -.
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 VEuPathDB; HostDB:ENSMUSG00000030963; -.
DR eggNOG; ENOG502QT6B; Eukaryota.
DR GeneTree; ENSGT00940000156742; -.
DR HOGENOM; CLU_028679_0_0_1; -.
DR InParanoid; Q91X17; -.
DR OMA; LECGVND; -.
DR OrthoDB; 665331at2759; -.
DR PhylomeDB; Q91X17; -.
DR TreeFam; TF330284; -.
DR Reactome; R-MMU-446203; Asparagine N-linked glycosylation.
DR BioGRID-ORCS; 22242; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Umod; mouse.
DR PRO; PR:Q91X17; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91X17; protein.
DR Bgee; ENSMUSG00000030963; Expressed in adult mammalian kidney and 59 other tissues.
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:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0019864; F:IgG binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0006914; P:autophagy; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IDA:MGI.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:MGI.
DR GO; GO:0034620; P:cellular response to unfolded protein; IMP:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:MGI.
DR GO; GO:0048878; P:chemical homeostasis; IMP:MGI.
DR GO; GO:0055064; P:chloride ion homeostasis; IMP:MGI.
DR GO; GO:0046720; P:citric acid secretion; IMP:MGI.
DR GO; GO:0072044; P:collecting duct development; IMP:MGI.
DR GO; GO:0097709; P:connective tissue replacement; IMP:MGI.
DR GO; GO:0097273; P:creatinine homeostasis; IMP:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0003094; P:glomerular filtration; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0050801; P:ion homeostasis; IMP:UniProtKB.
DR GO; GO:0072051; P:juxtaglomerular apparatus development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0072070; P:loop of Henle development; IMP: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:0060073; P:micturition; IMP:MGI.
DR GO; GO:0048871; P:multicellular organismal homeostasis; IMP:MGI.
DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
DR GO; GO:1990266; P:neutrophil migration; ISO:MGI.
DR GO; GO:0002251; P:organ or tissue specific immune response; IMP:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IMP:MGI.
DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:MGI.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR GO; GO:0072665; P:protein localization to vacuole; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0044861; P:protein transport into plasma membrane raft; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0051223; P:regulation of protein transport; IMP:MGI.
DR GO; GO:0035809; P:regulation of urine volume; IMP:MGI.
DR GO; GO:0070294; P:renal sodium ion absorption; IDA:MGI.
DR GO; GO:0097744; P:renal urate salt excretion; IMP:MGI.
DR GO; GO:0003091; P:renal water homeostasis; IMP:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0006986; P:response to unfolded protein; IMP:MGI.
DR GO; GO:0009414; P:response to water deprivation; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0008380; P:RNA splicing; IMP:MGI.
DR GO; GO:0055078; P:sodium ion homeostasis; IMP:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:MGI.
DR GO; GO:0015747; P:urate transport; IMP:MGI.
DR GO; GO:0071918; P:urea transmembrane transport; IMP:MGI.
DR GO; GO:0030104; P:water homeostasis; IMP:MGI.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; IPR042235; ZP-C.
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; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT CHAIN 25..618
FT /note="Uromodulin"
FT /id="PRO_0000041673"
FT CHAIN 25..588
FT /note="Uromodulin, secreted form"
FT /id="PRO_0000407910"
FT PROPEP 619..642
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041674"
FT DOMAIN 28..64
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 65..106
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 107..148
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 335..590
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 335..430
FT /note="ZP-N"
FT /evidence="ECO:0000255"
FT REGION 431..454
FT /note="Flexible linker; important for secretion and
FT polymerization into filaments"
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT REGION 455..465
FT /note="Internal hydrophobic patch (IHP)"
FT /evidence="ECO:0000255"
FT REGION 466..590
FT /note="ZP-C"
FT /evidence="ECO:0000255"
FT REGION 587..590
FT /note="Essential for cleavage by HPN"
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT REGION 599..608
FT /note="Regulates polymerization into filaments"
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT SITE 588..589
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:18375198,
FT ECO:0000269|PubMed:26673890"
FT LIPID 618
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 35..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 52..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 69..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 77..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 93..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 111..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 119..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 136..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 298..307
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 301..316
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 318..348
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 336..426
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 367..390
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 507..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 528..583
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 572..579
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT CONFLICT 22
FT /note="E -> G (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..104
FT /note="ELS -> GLG (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="E -> K (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="G -> S (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="L -> Q (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="R -> A (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="Q -> H (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> E (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="D -> G (in Ref. 2; BAE38225)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="H -> Y (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="S -> C (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="T -> TRQ (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..617
FT /note="Missing (in Ref. 1; AAA73896)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="P -> L (in Ref. 1; AAA73896)"
FT /evidence="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
