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Database: UniProt
Entry: V9KHG9_CALMI
LinkDB: V9KHG9_CALMI
Original site: V9KHG9_CALMI 
ID   V9KHG9_CALMI            Unreviewed;       561 AA.
AC   V9KHG9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Epidermal growth factor-like protein 6 {ECO:0000313|EMBL:AFO97806.1};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO97806.1};
RN   [1] {ECO:0000313|EMBL:AFO97806.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen {ECO:0000313|EMBL:AFO97806.1};
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
CC   -!- SIMILARITY: Belongs to the nephronectin family.
CC       {ECO:0000256|ARBA:ARBA00009738}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; JW865289; AFO97806.1; -; mRNA.
DR   AlphaFoldDB; V9KHG9; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR000998; MAM_dom.
DR   PANTHER; PTHR24050:SF20; -; 1.
DR   PANTHER; PTHR24050; PA14 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00629; MAM; 1.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00137; MAM; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50060; MAM_2; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..561
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004777776"
FT   DOMAIN          63..98
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          100..139
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          180..218
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          225..265
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          411..555
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DISULFID        88..97
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   561 AA;  62393 MW;  3AAF6C97D5395ACC CRC64;
     MKMWALFVKV LTVSSLSLWA AAEQSTSTSS SSSSRVRKLR STSGGFCRYG LRVDCCWGWN
     RRSWGHCQPV CQHGCKHGEC VGPNKCKCYP GYTGKTCNQD LNECGLKPRP CKHRCMNTYG
     SYKCYCLNGY MLMPDGSCAN TMSCLMANCQ YGCDEVKGEI RCRCPSSGLK LGPDRRTCVD
     VDECATGRVM CPRLRKCINT FGSYFCKCHD GFELRYFNGK YRCVDIDECS RRTHKCSAFA
     ACQNTPGSYK CKCFSGYKGS GYTCTYDPRT NKFPYLPPGN GRNETNGGMN SIPNDNNGNV
     RTIAPPRITV TPQHIPRTPE VRPAPTTARI TTTAGATTTI STTTAFTPAV PSTTVKSVDN
     RIHNEVPPQR GDVFIPRQPG GNGALIGLLD IEKGITAEEN DARDDQDILV SSCNFDHGMC
     GWTQEKRADL HWERVLSPLG RSWYLALSES NTKKRDVAHL ILPLALRAGT DNLCLTFRHK
     LSGDSLGKIQ VFMRRNSVYG QALWQRNRGY GWRTSRFTLK GPGIEHVIFK GVRETERSGE
     IALDDISLQR GHCSGKQQGL W
//
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