ID A0A7J7Z8G6_MYOMY Unreviewed; 987 AA.
AC A0A7J7Z8G6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 1 {ECO:0000256|ARBA:ARBA00067369};
DE AltName: Full=Signal peptide, CUB and EGF-like domain-containing protein 2 {ECO:0000256|ARBA:ARBA00067359};
GN ORFNames=mMyoMyo1_017154 {ECO:0000313|EMBL:KAF6370471.1};
OS Myotis myotis (Greater mouse-eared bat) (Vespertilio myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6370471.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6370471.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6370471.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6370471.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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:0000256|ARBA:ARBA00054446}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell
CC surface {ECO:0000256|ARBA:ARBA00004241}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6370471.1}.
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DR EMBL; JABWUV010000003; KAF6370471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J7Z8G6; -.
DR VEuPathDB; HostDB:GeneID_118651687; -.
DR Proteomes; UP000527355; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009967; P:positive regulation of signal transduction; IEA:UniProtKB-ARBA.
DR GO; GO:0007165; P:signal transduction; IEA:TreeGrafter.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 2.
DR FunFam; 2.10.50.10:FF:000024; signal peptide, CUB and EGF-like domain-containing protein 1; 1.
DR FunFam; 2.10.25.10:FF:000032; signal peptide, CUB and EGF-like domain-containing protein 2 isoform X1; 1.
DR FunFam; 2.10.25.10:FF:000199; signal peptide, CUB and EGF-like domain-containing protein 2 isoform X2; 1.
DR FunFam; 2.10.50.10:FF:000006; Signal peptide, CUB domain and EGF like domain containing 3; 1.
DR FunFam; 2.10.25.10:FF:000110; Signal peptide, CUB domain and EGF-like domain-containing 1; 1.
DR FunFam; 2.10.50.10:FF:000022; Signal peptide, CUB domain and EGF-like domain-containing 1; 1.
DR FunFam; 2.10.25.10:FF:000028; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000030; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000035; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000037; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.60.120.290:FF:000002; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000124; Signal peptide, CUB domain and EGF-like domain-containing 3; 1.
DR FunFam; 2.10.25.10:FF:000008; Signal peptide, CUB domain, EGF-like 2; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR024731; NELL2-like_EGF.
DR InterPro; IPR049883; NOTCH1_EGF-like.
DR InterPro; IPR052071; SCUB_EGF-like_domain.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR24046; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR24046:SF4; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 1; 1.
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 Pfam; PF14670; FXa_inhibition; 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; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000527355};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..987
FT /note="Signal peptide, CUB and EGF-like domain-containing
FT protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029882721"
FT DOMAIN 33..73
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 117..153
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 323..361
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 797..909
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 459..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 327..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 987 AA; 107661 MW; 8CBA521F2A70AC04 CRC64;
MGAAAVRWHL CVLLALGARG QLAAGSGLPG DVDVDECSEG TDECHIDAIC QNTPKSYRCL
CKPGFKGEGR KCEDIDECEN DSYNGGCVHE CINIPGNYRC TCFDGFMLAH DGHNCLDVDE
CQDNNGGCQQ ICVNALGSYE CQCHSGFFLS DNQHTCIHRS NEGMNCMNKD HGCAHICRET
PKGGVACDCR PGFDLAQNQK DCTLTCNYGN GGCQHSCEDT DTGPMCGCHQ KYALHSDGRT
CIETCAVNNG GCDRTCKDTA TGVRCSCPVG FTLQPDGKTC KDINECLANN GGCDHSCRNT
VGSFECGCRK GYKLLTDERT CQDVDECSFA RTCDHICVNS PGSFQCVCHR GYTLYGTTHC
GDVDECSMSN GSCDQGCVNT KGSFECVCPP GRRLHWNRKD CVDTGRCLSP AKAFPRAQLW
CSKTGGVESC SLACPAHTHF VPDSENSYSL SCGVPSLQGR TPQKRNGTSS STGPSCAGAP
ATPIRQKARF KIRDAKCHLR PRSREPVKEA PRQLLLENSH VTFVTLKCDS SKKRRRGRKS
PSKEVTHITA ELEVETKEEA SDTCEADCVR RRAEQSVQAA IRTLRKAVSR QLFSIQVAGT
EYEVAQQPAK APEGQGTCST GQTLQDSTCV ACEPGSYFSG DPGQCVPCAP GTYQDGEGQL
SCTPCPSSDG LGLAGARNVS ECGGQCSPGS FSADGFRPCQ ACPVGTYQPE PGRTSCFPCG
GGLLTKHEGM ASFQDCEAKV HCSPGHHYNT TSHRCIRCPI GTYQPEFGQN HCITCPGNTS
TDFDGSTNVT HCKNQHCGGE LGDYMGYIES PNYPGDYPAN AECVWYISPP PKRRILIVVP
EIFLPAEDEC GDALVMRKSA SPTSITTYET CQTYERPIAF TSRSRKLWIQ FRSNEGNSGK
GFQVPYVTYD EDYQQLIEDI VRDGRLYASE NHQEILKDKK LIKALFDVLA HPQNYFKYTA
QESKEMFPRS FIKLLRSKVS RFLRPYK
//
