SCUB1_MOUSE
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 03-AUG-2022, entry version 142.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., 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] (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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Could function as an adhesive molecule and its matrix bound
CC and soluble fragments may play a critical role in vascular biology.
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms homooligomers and heterooligomers with SCUBE2 and
CC SCUBE3. {ECO:0000250|UniProtKB:Q8IWY4}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IWY4}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8IWY4}; Peripheral membrane protein
CC {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 gonad,
CC 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}.
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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 AlphaFoldDB; Q6NZL8; -.
DR BioGRID; 211102; 2.
DR IntAct; Q6NZL8; 3.
DR MINT; Q6NZL8; -.
DR STRING; 10090.ENSMUSP00000016907; -.
DR GlyConnect; 2712; 4 N-Linked glycans (2 sites).
DR GlyGen; Q6NZL8; 7 sites, 4 N-linked glycans (2 sites).
DR PhosphoSitePlus; Q6NZL8; -.
DR MaxQB; Q6NZL8; -.
DR PaxDb; Q6NZL8; -.
DR PRIDE; Q6NZL8; -.
DR ProteomicsDB; 255499; -. [Q6NZL8-1]
DR ProteomicsDB; 255500; -. [Q6NZL8-2]
DR ProteomicsDB; 255501; -. [Q6NZL8-3]
DR Antibodypedia; 306; 100 antibodies from 22 providers.
DR DNASU; 64706; -.
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 VEuPathDB; HostDB:ENSMUSG00000016763; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000153185; -.
DR HOGENOM; CLU_013079_0_0_1; -.
DR InParanoid; Q6NZL8; -.
DR OMA; CSMSNGS; -.
DR OrthoDB; 73164at2759; -.
DR PhylomeDB; Q6NZL8; -.
DR TreeFam; TF351672; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 64706; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Scube1; mouse.
DR PRO; PR:Q6NZL8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6NZL8; protein.
DR Bgee; ENSMUSG00000016763; Expressed in hindlimb bud and 85 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; 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 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; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1018
FT /note="Signal peptide, CUB and EGF-like domain-containing
FT protein 1"
FT /id="PRO_0000254649"
FT DOMAIN 33..73
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 74..116
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 117..153
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 166..202
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 206..241
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 275..310
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 312..352
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 353..391
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 392..428
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 828..940
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 493..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..50
FT /evidence="ECO:0000250"
FT DISULFID 44..59
FT /evidence="ECO:0000250"
FT DISULFID 61..72
FT /evidence="ECO:0000250"
FT DISULFID 78..91
FT /evidence="ECO:0000250"
FT DISULFID 87..100
FT /evidence="ECO:0000250"
FT DISULFID 102..115
FT /evidence="ECO:0000250"
FT DISULFID 121..132
FT /evidence="ECO:0000250"
FT DISULFID 128..141
FT /evidence="ECO:0000250"
FT DISULFID 316..327
FT /evidence="ECO:0000250"
FT DISULFID 323..336
FT /evidence="ECO:0000250"
FT DISULFID 338..351
FT /evidence="ECO:0000250"
FT DISULFID 357..367
FT /evidence="ECO:0000250"
FT DISULFID 363..376
FT /evidence="ECO:0000250"
FT DISULFID 378..390
FT /evidence="ECO:0000250"
FT DISULFID 396..407
FT /evidence="ECO:0000250"
FT DISULFID 403..416
FT /evidence="ECO:0000250"
FT DISULFID 828..854
FT /evidence="ECO:0000250"
FT DISULFID 881..902
FT /evidence="ECO:0000250"
FT VAR_SEQ 244..273
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11087664,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021271"
FT VAR_SEQ 942..991
FT /note="EDYQQLIEDIVRDGRLYASENHQEILKDKKLIKALFDVLAHPQNYFKYTA
FT -> GKSPPSCHSPLCASQGLAWGLRNELHIPASDRAQTQRQKLGLGNAETQGV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11087664"
FT /id="VSP_021272"
FT VAR_SEQ 992..1018
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11087664"
FT /id="VSP_021273"
FT CONFLICT 11
FT /note="Y -> S (in Ref. 1; AAG25939)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="R -> Q (in Ref. 1; AAG25939)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="K -> R (in Ref. 1; AAG25939)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="I -> T (in Ref. 1; AAG25939)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="G -> V (in Ref. 3; AAH66066)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="D -> DGRLP (in Ref. 2; BAC30996)"
FT /evidence="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
