GenomeNet

Database: UniProt
Entry: Q6NZL8
LinkDB: Q6NZL8
Original site: Q6NZL8 
ID   SCUB1_MOUSE             Reviewed;        1018 AA.
AC   Q6NZL8; Q8C9Q4; Q9EQC6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   10-APR-2019, entry version 125.
DE   RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Scube1;
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] (ISOFORM 3), AND DEVELOPMENTAL STAGE.
RC   STRAIN=C3H/HeJ;
RX   PubMed=11087664; DOI=10.1006/geno.2000.6370;
RA   Grimmond S., Larder R., Van Hateren N., Siggers P., Hulsebos T.J.M.,
RA   Arkell R., Greenfield A.;
RT   "Cloning, mapping, and expression analysis of a gene encoding a novel
RT   mammalian EGF-related protein (SCUBE1).";
RL   Genomics 70:74-81(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC   -!- FUNCTION: Could function as an adhesive molecule and its matrix
CC       bound and soluble fragments may play a critical role in vascular
CC       biology. {ECO:0000250}.
CC   -!- SUBUNIT: Forms homooligomers and heterooligomers with SCUBE2 and
CC       SCUBE3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IWY4}.
CC       Cell membrane {ECO:0000250|UniProtKB:Q8IWY4}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:Q8IWY4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6NZL8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NZL8-2; Sequence=VSP_021271;
CC       Name=3;
CC         IsoId=Q6NZL8-3; Sequence=VSP_021271, VSP_021272, VSP_021273;
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly in the developing
CC       gonad, nervous system somites, surface ectoderm and limb buds.
CC       {ECO:0000269|PubMed:11087664}.
CC   -!- INDUCTION: Down-regulated by inflammatory cytokines.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: Could be proteolytically cleaved to release a smaller active
CC       fragment. {ECO:0000250}.
DR   EMBL; AF276425; AAG25939.1; -; mRNA.
DR   EMBL; AK041590; BAC30996.1; -; mRNA.
DR   EMBL; BC066066; AAH66066.1; -; mRNA.
DR   CCDS; CCDS49684.1; -. [Q6NZL8-2]
DR   CCDS; CCDS70655.1; -. [Q6NZL8-1]
DR   RefSeq; NP_001258401.1; NM_001271472.1. [Q6NZL8-1]
DR   RefSeq; NP_073560.2; NM_022723.3. [Q6NZL8-2]
DR   UniGene; Mm.40393; -.
DR   ProteinModelPortal; Q6NZL8; -.
DR   SMR; Q6NZL8; -.
DR   IntAct; Q6NZL8; 1.
DR   MINT; Q6NZL8; -.
DR   STRING; 10090.ENSMUSP00000016907; -.
DR   PhosphoSitePlus; Q6NZL8; -.
DR   PaxDb; Q6NZL8; -.
DR   PRIDE; Q6NZL8; -.
DR   Ensembl; ENSMUST00000016907; ENSMUSP00000016907; ENSMUSG00000016763. [Q6NZL8-1]
DR   Ensembl; ENSMUST00000171496; ENSMUSP00000130131; ENSMUSG00000016763. [Q6NZL8-2]
DR   GeneID; 64706; -.
DR   KEGG; mmu:64706; -.
DR   UCSC; uc007xbi.2; mouse. [Q6NZL8-2]
DR   UCSC; uc007xbj.2; mouse. [Q6NZL8-1]
DR   CTD; 80274; -.
DR   MGI; MGI:1890616; Scube1.
DR   eggNOG; ENOG410IR7D; Eukaryota.
DR   eggNOG; ENOG411030G; LUCA.
DR   GeneTree; ENSGT00940000153185; -.
DR   HOGENOM; HOG000230943; -.
DR   HOVERGEN; HBG054902; -.
DR   InParanoid; Q6NZL8; -.
DR   OMA; SINKQQF; -.
DR   OrthoDB; 73164at2759; -.
DR   TreeFam; TF351672; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   PRO; PR:Q6NZL8; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000016763; Expressed in 97 organ(s), highest expression level in visual cortex.
DR   ExpressionAtlas; Q6NZL8; baseline and differential.
DR   Genevisible; Q6NZL8; MM.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   CDD; cd00041; CUB; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR000859; CUB_dom.
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; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF07699; Ephrin_rec_like; 3.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM01411; Ephrin_rec_like; 3.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF57184; SSF57184; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 6.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cell membrane; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21   1018       Signal peptide, CUB and EGF-like domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000254649.
FT   DOMAIN       33     73       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN       74    116       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      117    153       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      166    202       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      206    241       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      275    310       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      312    352       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      353    391       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      392    428       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      828    940       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   CARBOHYD    255    255       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    400    400       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    496    496       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    709    709       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    780    780       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    809    809       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    819    819       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     37     50       {ECO:0000250}.
FT   DISULFID     44     59       {ECO:0000250}.
FT   DISULFID     61     72       {ECO:0000250}.
FT   DISULFID     78     91       {ECO:0000250}.
FT   DISULFID     87    100       {ECO:0000250}.
FT   DISULFID    102    115       {ECO:0000250}.
FT   DISULFID    121    132       {ECO:0000250}.
FT   DISULFID    128    141       {ECO:0000250}.
FT   DISULFID    316    327       {ECO:0000250}.
FT   DISULFID    323    336       {ECO:0000250}.
FT   DISULFID    338    351       {ECO:0000250}.
FT   DISULFID    357    367       {ECO:0000250}.
FT   DISULFID    363    376       {ECO:0000250}.
FT   DISULFID    378    390       {ECO:0000250}.
FT   DISULFID    396    407       {ECO:0000250}.
FT   DISULFID    403    416       {ECO:0000250}.
FT   DISULFID    828    854       {ECO:0000250}.
FT   DISULFID    881    902       {ECO:0000250}.
FT   VAR_SEQ     244    273       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:11087664,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021271.
FT   VAR_SEQ     942    991       EDYQQLIEDIVRDGRLYASENHQEILKDKKLIKALFDVLAH
FT                                PQNYFKYTA -> GKSPPSCHSPLCASQGLAWGLRNELHIP
FT                                ASDRAQTQRQKLGLGNAETQGV (in isoform 3).
FT                                {ECO:0000303|PubMed:11087664}.
FT                                /FTId=VSP_021272.
FT   VAR_SEQ     992   1018       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11087664}.
FT                                /FTId=VSP_021273.
FT   CONFLICT     11     11       Y -> S (in Ref. 1; AAG25939).
FT                                {ECO:0000305}.
FT   CONFLICT     21     21       R -> Q (in Ref. 1; AAG25939).
FT                                {ECO:0000305}.
FT   CONFLICT    411    411       K -> R (in Ref. 1; AAG25939).
FT                                {ECO:0000305}.
FT   CONFLICT    619    619       I -> T (in Ref. 1; AAG25939).
FT                                {ECO:0000305}.
FT   CONFLICT    833    833       G -> V (in Ref. 3; AAH66066).
FT                                {ECO:0000305}.
FT   CONFLICT    941    941       D -> DGRLP (in Ref. 2; BAC30996).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1018 AA;  111606 MW;  1F4B3EDF84F0CC42 CRC64;
     MGAAAVRWHL YLLLALGARG RLVGGSGLPG AVDVDECSEG TDDCHIDAIC QNTPKSYKCL
     CKPGYKGEGR QCEDIDECEN DYYNGGCVHD CINIPGNYRC TCFDGFMLAH DGHNCLDVDE
     CQDNNGGCQQ ICVNAMGSYE CQCHSGFFLS DNQHTCIHRS NEGMNCMNKD HGCAHICRET
     PKGGVACDCR PGFDLAQNQK DCTLTCNYGN GGCQHSCEDT DTGPMCGCHQ KYALHADGRT
     CIEKDEAAIE RSQFNATSVA DVDKRVKRRL LMETCAVNNG GCDRTCKDTA TGVRCSCPVG
     FTLQPDGKTC KDINECLMNN GGCDHFCRNT VGSFECGCQK GHKLLTDERT CQDIDECSFE
     RTCDHICINS PGSFQCLCRR GYTLYGTTHC GDVDECSMNN GSCEQGCVNT KGSYECVCPP
     GRRLHWNQKD CVEMNGCLSR SKASAQAQLS CGKVGGVENC FLSCLGHSLF MPDSESSYIL
     SCGVPGLQGK TLPKRNGTSS STGPGCSDAP TTPIRQKARF KIRDAKCHLQ PRSQERAKDT
     LRHPLLDNCH VTFVTLKCDS SKKRRRGRKS PSKEVSHITA EFEVEMKVDE ASGTCEADCM
     RKRAEQSLQA AIKILRKSIG RNQFYVQVLG TEYEVAQRPA KALEGTGTCG IGQILQDGKC
     VPCAPGTYFS GDPGQCMPCV SGTYQDMEGQ LSCTPCPSSE GLGLAGARNV SECGGQCSPG
     YFSADGFKPC QACPVGTYQP EPGRTGCFPC GGGLLTKHTG TASFQDCEAK VHCSPGHHYN
     TTTHRCIRCP VGTYQPEFGQ NHCISCPGNT STDFDGSTNV THCKNQHCGG ELGDYTGYIE
     SPNYPGDYPA NAECVWHIAP PPKRRILIVV PEIFLPIEDE CGDVLVMRKS ASPTSVTTYE
     TCQTYERPIA FTSRSRKLWI QFKSNEANSG KGFQVPYVTY DEDYQQLIED IVRDGRLYAS
     ENHQEILKDK KLIKALFDVL AHPQNYFKYT AQESKEMFPR SFIKLLRSKV SRFLRPYK
//
DBGET integrated database retrieval system