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Nephronectin (Preosteoblast EGF-like repeat protein with MAM domain)

 NPNT_MOUSE              Reviewed;         561 AA.
Q91V88; Q6NV58; Q80VP6; Q91XL5; Q91ZD3; Q923T5;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
20-JUN-2018, entry version 135.
RecName: Full=Nephronectin;
AltName: Full=Preosteoblast EGF-like repeat protein with MAM domain;
Flags: Precursor;
Name=Npnt; Synonyms=Neph1, Poem;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, OLIGOMERIZATION,
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ASP-384.
STRAIN=C57BL/6J; TISSUE=Preosteoblast;
PubMed=11546798; DOI=10.1074/jbc.M103216200;
Morimura N., Tezuka Y., Watanabe N., Yasuda M., Miyatani S.,
Hozumi N., Tezuka Ki K.;
"Molecular cloning of POEM: a novel adhesion molecule that interacts
with alpha8beta1 integrin.";
J. Biol. Chem. 276:42172-42181(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J, and NIH Swiss; TISSUE=Kidney;
PubMed=11470831; DOI=10.1083/jcb.200103069;
Brandenberger R., Schmidt A., Linton J., Wang D., Backus C., Denda S.,
Mueller U., Reichardt L.F.;
"Identification and characterization of a novel extracellular matrix
protein nephronectin that is associated with integrin alpha8beta1 in
the embryonic kidney.";
J. Cell Biol. 154:447-458(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Kidney, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17537792; DOI=10.1242/dev.005033;
Linton J.M., Martin G.R., Reichardt L.F.;
"The ECM protein nephronectin promotes kidney development via integrin
alpha8beta1-mediated stimulation of Gdnf expression.";
Development 134:2501-2509(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Functional ligand of integrin alpha-8/beta-1 in kidney
development. Regulates the expression of GDNF with integrin alpha-
8/beta-1 which is essential for kidney development. May also play
a role in the development and function of various tissues,
regulating cell adhesion, spreading and survival through the
binding of several integrins. {ECO:0000269|PubMed:11470831,
ECO:0000269|PubMed:11546798, ECO:0000269|PubMed:17537792}.
-!- SUBUNIT: Homodimer and homotrimer.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11546798}.
Note=Trapped on the cell surface or in the extracellular matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Short;
IsoId=Q91V88-1; Sequence=Displayed;
Name=2; Synonyms=Long;
IsoId=Q91V88-2; Sequence=VSP_026989;
Name=3;
IsoId=Q91V88-3; Sequence=VSP_026990;
Name=4;
IsoId=Q91V88-4; Sequence=VSP_026989, VSP_026990;
-!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
{ECO:0000269|PubMed:11470831}.
-!- DEVELOPMENTAL STAGE: Expressed from 10.5 dpc onward mainly at
epithelial-mesenchymal interfaces in kidney and other tissues
undergoing morphogenesis (at protein level).
{ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11546798}.
-!- DOMAIN: The MAM domain is required for localization at the cell
surface.
-!- DISRUPTION PHENOTYPE: Mice display renal agenesis at birth due to
a developmental delay. This delay is associated with a reduced
expression of Gdnf and is similar to the one found in mice lacking
Itga8. {ECO:0000269|PubMed:17537792}.
-!- MISCELLANEOUS: Was named nephronectin based on its potential role
in kidney development.
-!- SIMILARITY: Belongs to the nephronectin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB059656; BAB69692.1; -; mRNA.
EMBL; AF397007; AAK84391.1; -; mRNA.
EMBL; AF397008; AAK84392.1; -; mRNA.
EMBL; AY035898; AAK96010.1; -; mRNA.
EMBL; AY035899; AAK96011.1; -; mRNA.
EMBL; AK050484; BAC34283.1; -; mRNA.
EMBL; BC046642; AAH46642.1; -; mRNA.
EMBL; BC068308; AAH68308.1; -; mRNA.
CCDS; CCDS17845.1; -. [Q91V88-1]
CCDS; CCDS17846.1; -. [Q91V88-2]
CCDS; CCDS71322.1; -. [Q91V88-3]
CCDS; CCDS71323.1; -. [Q91V88-4]
RefSeq; NP_001025007.1; NM_001029836.2. [Q91V88-1]
RefSeq; NP_001274030.1; NM_001287101.1. [Q91V88-4]
RefSeq; NP_001274031.1; NM_001287102.1. [Q91V88-3]
RefSeq; NP_277060.2; NM_033525.3. [Q91V88-2]
UniGene; Mm.279310; -.
UniGene; Mm.440226; -.
ProteinModelPortal; Q91V88; -.
SMR; Q91V88; -.
IntAct; Q91V88; 2.
STRING; 10090.ENSMUSP00000040071; -.
iPTMnet; Q91V88; -.
PhosphoSitePlus; Q91V88; -.
PaxDb; Q91V88; -.
PRIDE; Q91V88; -.
Ensembl; ENSMUST00000042729; ENSMUSP00000040071; ENSMUSG00000040998. [Q91V88-2]
Ensembl; ENSMUST00000042744; ENSMUSP00000040684; ENSMUSG00000040998. [Q91V88-1]
Ensembl; ENSMUST00000093971; ENSMUSP00000091505; ENSMUSG00000040998. [Q91V88-4]
Ensembl; ENSMUST00000117164; ENSMUSP00000113419; ENSMUSG00000040998. [Q91V88-3]
GeneID; 114249; -.
KEGG; mmu:114249; -.
UCSC; uc008rkc.3; mouse. [Q91V88-2]
UCSC; uc008rkd.3; mouse. [Q91V88-1]
UCSC; uc008rke.3; mouse. [Q91V88-4]
UCSC; uc008rkf.3; mouse. [Q91V88-3]
CTD; 255743; -.
MGI; MGI:2148811; Npnt.
eggNOG; ENOG410IR6Z; Eukaryota.
eggNOG; ENOG411039V; LUCA.
GeneTree; ENSGT00920000149031; -.
HOGENOM; HOG000059638; -.
HOVERGEN; HBG108200; -.
InParanoid; Q91V88; -.
KO; K06824; -.
OMA; CPRFRQC; -.
OrthoDB; EOG091G02IF; -.
PhylomeDB; Q91V88; -.
TreeFam; TF330819; -.
PRO; PR:Q91V88; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000040998; -.
CleanEx; MM_NPNT; -.
ExpressionAtlas; Q91V88; baseline and differential.
Genevisible; Q91V88; MM.
GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0030485; C:smooth muscle contractile fiber; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005178; F:integrin binding; IDA:BHF-UCL.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IDA:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:BHF-UCL.
GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
GO; GO:0097195; P:pilomotor reflex; IMP:BHF-UCL.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IDA:BHF-UCL.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:BHF-UCL.
GO; GO:2000721; P:positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
GO; GO:0001657; P:ureteric bud development; IMP:MGI.
CDD; cd06263; MAM; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR000998; MAM_dom.
Pfam; PF07645; EGF_CA; 3.
Pfam; PF00629; MAM; 1.
SMART; SM00181; EGF; 5.
SMART; SM00179; EGF_CA; 3.
SMART; SM00137; MAM; 1.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS50060; MAM_2; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell adhesion; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
EGF-like domain; Extracellular matrix; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 561 Nephronectin.
/FTId=PRO_0000295685.
DOMAIN 52 87 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 89 128 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 132 168 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 169 213 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 214 254 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 420 561 MAM. {ECO:0000255|PROSITE-
ProRule:PRU00128}.
MOTIF 382 384 Integrin interaction.
COMPBIAS 296 359 Pro-rich.
DISULFID 56 69 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 60 75 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 77 86 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 93 104 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 100 113 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 115 127 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 173 186 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 180 195 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 197 212 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 218 231 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 225 240 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 242 253 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VAR_SEQ 58 58 P -> PFYVLRQRLARIRCQLKA (in isoform 2 and
isoform 4).
{ECO:0000303|PubMed:11470831}.
/FTId=VSP_026989.
VAR_SEQ 88 88 Q -> QDESFHPTPLDQGSEQPLFQPPDHQATNVPSR (in
isoform 3 and isoform 4).
{ECO:0000303|PubMed:11470831}.
/FTId=VSP_026990.
MUTAGEN 384 384 D->E: Reduced cell spreading- and
survival-promoting activities.
{ECO:0000269|PubMed:11546798}.
CONFLICT 24 24 R -> G (in Ref. 4; AAH68308).
{ECO:0000305}.
SEQUENCE 561 AA; 61490 MW; 69E7ACAA0EE3F506 CRC64;
MAVLLAAVLA SSLYLQVAAD FDGRWPRQIV SSIGLCRYGG RIDCCWGWAR QSWGQCQPVC
QPQCKHGECV GPNKCKCHPG FAGKTCNQDL NECGLKPRPC KHRCMNTFGS YKCYCLNGYM
LLPDGSCSSA LSCSMANCQY GCDVVKGQVR CQCPSPGLQL APDGRTCVDI DECATGRVSC
PRFRQCVNTF GSYICKCHTG FDLMYIGGKY QCHDIDECSL GQHQCSSYAR CYNIHGSYKC
QCRDGYEGDG LNCVYIPKVM IEPSGPIHMP ERNGTISKGD GGHANRIPDA GSTRWPLKTP
YIPPVITNRP TSKPTTRPTP NPTPQPTPPP PPPLPTEPRT TPLPPTPERP STRPTTIAPA
TSTTTRVITV DNRIQTDPQK PRGDVFIPRQ PTNDLFEIFE IERGVSADEE VKDDPGILIH
SCNFDHGLCG WIREKDSDLH WETARDPAGG QYLTVSAAKA PGGKAARLVL RLGHLMHSGD
LCLSFRHKVT GLHSGTLQVF VRKHGTHGAA LWGRNGGHGW RQTQITLRGA DVKSVIFKGE
KRRGHTGEIG LDDVSLKRGR C


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