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Protein HEG homolog 1

 HEG1_MOUSE              Reviewed;        1337 AA.
E9Q7X6; Q3TR26; Q6GQS6; Q8CED0;
25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
25-APR-2018, entry version 52.
RecName: Full=Protein HEG homolog 1;
Flags: Precursor;
Name=Heg1;
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 [LARGE SCALE MRNA] (ISOFORM 3).
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1007-1240 (ISOFORM 1).
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]
IDENTIFICATION, FUNCTION, INTERACTION WITH CCM2 AND KRIT1, SUBCELLULAR
LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=19151727; DOI=10.1038/nm.1918;
Kleaveland B., Zheng X., Liu J.J., Blum Y., Tung J.J., Zou Z.,
Sweeney S.M., Chen M., Guo L., Lu M.M., Zhou D., Kitajewski J.,
Affolter M., Ginsberg M.H., Kahn M.L.;
"Regulation of cardiovascular development and integrity by the heart
of glass-cerebral cavernous malformation protein pathway.";
Nat. Med. 15:169-176(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1315, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Lung, and Spleen;
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: Receptor component of the CCM signaling pathway which is
a crucial regulator of heart and vessel formation and integrity.
May be acting by stabilizing endothelial cell junctions.
{ECO:0000269|PubMed:19151727}.
-!- SUBUNIT: Interacts with CCM2 and KRIT1; KRIT1 markedly facilitates
interaction with CCM2. {ECO:0000269|PubMed:19151727}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}. Cell junction
{ECO:0000269|PubMed:19151727}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=E9Q7X6-1; Sequence=Displayed;
Name=2;
IsoId=E9Q7X6-2; Sequence=VSP_042234;
Note=No experimental confirmation available.;
Name=3;
IsoId=E9Q7X6-3; Sequence=VSP_042234, VSP_042235, VSP_042236;
Note=May be due to an intron retention. No experimental
confirmation available.;
-!- DEVELOPMENTAL STAGE: Expressed in the endothelium of the
developing heart and aorta and in the neural tube at 10.5 dpc, and
in the arterial endothelium, smooth muscle, endocardium of the
heart and brain vasculature at 14.5 dpc.
{ECO:0000269|PubMed:19151727}.
-!- DISRUPTION PHENOTYPE: Some mutant animals die in utero, but most
die postnatally, about half before weaning as a result of
pulmonary hemorrhage. Midgestation mutant embryos show cardiac
defects characterized by invagination of the ventricular cavity
into, and often through, the compact layer of ventricular
myocardium. The septal myocardium is similarly honeycombed by
endothelial-lined extensions from the ventricular cavity, a defect
accompanied by the presence of ventricular septal defects in most
late-gestation embryos. Neonatal mice also show defective cardiac
integrity manifested by a blood-filled pericardial sac, due to the
rupture of the low-pressure atrial chamber of the heart. Cardiac
or pulmonary integrity defects are observed in half of the
animals. About 10% of neonatal mutant mice exhibit dilated
lymphatic vessel malformations. {ECO:0000269|PubMed:19151727}.
-!- SEQUENCE CAUTION:
Sequence=AAH72651.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AK163128; BAE37205.1; -; mRNA.
EMBL; AK028518; BAC25987.1; -; mRNA.
EMBL; AC121570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466521; EDK97850.1; -; Genomic_DNA.
EMBL; BC072651; AAH72651.1; ALT_INIT; mRNA.
UniGene; Mm.245741; -.
ProteinModelPortal; E9Q7X6; -.
CORUM; E9Q7X6; -.
STRING; 10090.ENSMUSP00000119790; -.
iPTMnet; E9Q7X6; -.
PhosphoSitePlus; E9Q7X6; -.
MaxQB; E9Q7X6; -.
PaxDb; E9Q7X6; -.
PRIDE; E9Q7X6; -.
Ensembl; ENSMUST00000126532; ENSMUSP00000119790; ENSMUSG00000075254. [E9Q7X6-1]
UCSC; uc007zah.1; mouse. [E9Q7X6-3]
MGI; MGI:1924696; Heg1.
eggNOG; ENOG410IJZT; Eukaryota.
eggNOG; ENOG410Y1MK; LUCA.
GeneTree; ENSGT00710000106813; -.
HOVERGEN; HBG070920; -.
InParanoid; E9Q7X6; -.
OMA; FWQNDSP; -.
OrthoDB; EOG091G09EZ; -.
PRO; PR:E9Q7X6; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000075254; -.
ExpressionAtlas; E9Q7X6; baseline and differential.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:MGI.
GO; GO:0055017; P:cardiac muscle tissue growth; IGI:MGI.
GO; GO:0007043; P:cell-cell junction assembly; IEA:InterPro.
GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
GO; GO:0001885; P:endothelial cell development; IGI:MGI.
GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0003017; P:lymph circulation; IMP:MGI.
GO; GO:0001945; P:lymph vessel development; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
GO; GO:0060039; P:pericardium development; IMP:MGI.
GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IGI:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0050878; P:regulation of body fluid levels; IMP:MGI.
GO; GO:0001944; P:vasculature development; IGI:MGI.
GO; GO:0001570; P:vasculogenesis; IGI:MGI.
GO; GO:0048845; P:venous blood vessel morphogenesis; IGI:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IGI:MGI.
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; IPR028720; HEG.
PANTHER; PTHR24037; PTHR24037; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF07645; EGF_CA; 1.
SMART; SM00181; EGF; 3.
SMART; SM00179; EGF_CA; 2.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell junction; Cell membrane;
Complete proteome; Developmental protein; Disulfide bond;
EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 1337 Protein HEG homolog 1.
/FTId=PRO_0000415377.
TOPO_DOM 32 1204 Extracellular. {ECO:0000255}.
TRANSMEM 1205 1225 Helical. {ECO:0000255}.
TOPO_DOM 1226 1337 Cytoplasmic. {ECO:0000255}.
DOMAIN 941 979 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 981 1019 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
COMPBIAS 482 697 Ser-rich.
MOD_RES 1315 1315 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 1093 1093 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 945 956 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 950 967 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 969 978 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 985 996 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 990 1005 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1007 1018 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VAR_SEQ 83 179 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_042234.
VAR_SEQ 510 550 LTGLSYTREHGSDAGQRTSSDHTDHGYVPSTFTKGERTLLS
-> REFLVHGNRHRVLGCVWSFDLPKHTLGKEFHYSQAIIL
LAD (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_042235.
VAR_SEQ 551 1337 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_042236.
SEQUENCE 1337 AA; 141899 MW; 80D24CAAC1AD77BF CRC64;
MATPRAPRWP PPSLLLLLLL PLLLLPPAAP GARGSLPSPA HRTLLPVAGP LSPPGAGHTA
PGPGVATRRG RSGRVPRGVS AAAARNRWLE SNNPEPHIGC SPSYQSQEDH SGSRKGVTAQ
NARMSHSSSE GPENPPLLPE TSAEWSNMAS SHRADIAGLR RGPSPEITTA PTAHSSLLSL
ESLPESPSSS RSQRRITPSQ TESGTSLGFL ERTRELPEEG TVHTQVAGTW VSRQASHPAL
EPGEPTVLSQ KRNSSGQEHS GPPFSWSQSH PPPSDHPSSS GSIKNGNNFT ALQNPSVTQT
KSMLITDTYT NGVPRTLRSL PVGVDPADET EGFPEHSRLG ITSMSVRSSP SVKDSRTNSG
LTEHLGDGEG TELSTENGYG LPSIHWQSDA PSFGGRQLAS SSEAGDGRAM PLTEAVFRSD
PSIGGGESTG RWILTKKKTS TDAAESSALH PEAGGAGGLT QSSHAAQQPR GGGEDSGMGG
RSYAESSSSS SSTSSSESLD SSAPLREHSL TGLSYTREHG SDAGQRTSSD HTDHGYVPST
FTKGERTLLS ITDNTSYSEA SESSTSSVKI SDSPSQAQPK QSSMSSDDDE PAQSSTESPV
LHTSNLPTYT STVNMPNTLV LDTGTKPVED PSDSRVPSTQ PSPSQPQPFS SALPSTRSPG
STSETTTSSP SPSPISLLVS TLAPYSVSQT TFPHPSSTLV PHRPREPRVT SVQMSTAISA
IALIPSNQTA NPKNQSTPQQ EKPITEAKSP SLVSPPTDST KAVTVSLPPG APWSPALTGF
STGPALPATS TSLAQMSPAL TSAMPQTTHS PVTSPSTLSH VEALTSGAVV VHTTPKKPHL
PTNPEILVPH ISTEGAITTE GNREHTDPTT QPIPLTTSTT SAGERTTELG RAEESSPSHF
LTPSSPQTTD VSTAEMLTSR YITFAAQSTS QSPTALPPLT PVNSCTVNPC LHDGKCIVDL
TGRGYRCVCP PAWQGENCSV DVNECLSSPC PPLATCNNTQ GSFTCRCPVG YQLEKGICNL
VRTFVTEFKL KKTFLNTTAE NHSNTQELEN EIAQTLNVCF STLPGYIRTT AHVSREPSTV
FISLKTTFAL ASNVTLFDLA DRIQKYVNSC RSSAEVCQLL GSQRRVFRAG SLCKRKSPEC
DKETSICTDL DGVALCQCKS GYFQFNKMDH SCRACEDGYR LENETCMSCP FGLGGLNCGN
PYQLITVVIA AAGGGLLLIL GVALIVTCCR KSKNDISKLI FKSGDFQMSP YTDVPKNPRS
QEWGREAIEM HENGSTKNLL QMTDVYYSPT NVRNPELERN GLYPAYTGLP GSRHSCIFPG
QYNPSFISDE SRRRDYF


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