ID A0A401RXV2_CHIPU Unreviewed; 1017 AA.
AC A0A401RXV2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=chiPu_0001320 {ECO:0000313|EMBL:GCC22929.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC22929.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC22929.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SUBCELLULAR LOCATION: Secreted {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:GCC22929.1}.
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DR EMBL; BEZZ01000020; GCC22929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RXV2; -.
DR STRING; 137246.A0A401RXV2; -.
DR OMA; CFFERAC; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 3.
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; 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 PANTHER; PTHR24046; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR24046:SF3; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF14670; FXa_inhibition; 4.
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; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 3.
PE 4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1017
FT /note="Signal peptide, CUB and EGF-like domain-containing
FT protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019510620"
FT DOMAIN 30..70
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 113..149
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 308..348
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 349..387
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 388..428
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 827..939
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 353..363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1017 AA; 113713 MW; B468526E2D8ABEA4 CRC64;
MGDICFAWHF CLFFLLLNSR ETSASAGILD IDECTEGTDD CHIDAICQNT QMLYKCTCKF
GYKGDGKKCE DIDECDNEYN GGCVHECINI PGNYRCTCYD GFMLAHDGHN CLDVDECIFN
NGGCQQTCVN TVGSYECQCK DGFFLSDNQH TCIHRSEEGM SCMNKEHGCA HICRETPKGG
IACECRPGFE LARNQRGCLL TCNHGNGGCH HTCDDTDDGP VCGCHQKYAL LSDGKICIEK
AEAAIENSEY NATSLTDVDK RVKRRLLMET CAVNNGGCDR TCKDTSTGVR CSCPVGFTLQ
PDGKTCKDID ECLNNNGDCD HFCKNTIGSF GCSCKKGYKL LTDERTCQDV DECFFERACD
HICINYPGHF ECVCKKGYTL YGLIHCGDVD ECSINNGGCE HRCMNSVGSY KCHCGPGYKL
HWNKKDCVEA EKLPPTKVSA KALLNCSKRG GADMCSLSCP SNVYFAAESE DSYTIRCGVS
SQCQHLDIPH CTGLNATILP IVKTTASFKI NAGRCELSRI KEKINSSLKQ ISSEKHNFPR
AKNCQLNFVN VKCSSFKRSH ENWKHQAMAN VGSIIYTVFE VEMKPEEVTE TCDFGCTRRK
TEKRLRKTTR TLRKSINREQ FYLRVAGTDY EVAKKTVKAV DLHEPCGTGQ VLQNNRCVSC
SVGTYYDGEQ KCILCPAGTY QDEEGQLSCE PCPNSDNQEN QKSPGARNVS ECGGQCLNGE
FSSDGFRPCQ SCPFGTYQPE FGRTSCFSCG GGLTTKREGA ASFQDCETKV QCSPGHFYDT
NTHRCIRCPI GLYQPEFGQN HCVACPGNTT TDFDGSTNIT QCKNRQCGGE LGDYTGYIES
PNYPGDYPAN VECTWNLSPP PKRRILIVVP EIFLPIDDEC GDYLVMRKSS LSNSVTTYET
CQTYERPIAF TSRSRKLWIQ FKSNEGNSDK GFQVPYVTYD EDYQELIEDI VRDGRLYASE
NHQEILKDKK LINALFDVLA HPQNYFKYTA QESREMFPRS FIRLLRSKVS RFLRPYK
//
