ID A0A3Q1INL8_ANATE Unreviewed; 520 AA.
AC A0A3Q1INL8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=EGF-like-domain, multiple 6 {ECO:0000313|Ensembl:ENSATEP00000019273.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000019273.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000019273.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q1INL8; -.
DR Ensembl; ENSATET00000019596.2; ENSATEP00000019273.1; ENSATEG00000013415.2.
DR GeneTree; ENSGT00930000150973; -.
DR OMA; NGRACID; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000998; MAM_dom.
DR PANTHER; PTHR24050:SF24; EPIDERMAL GROWTH FACTOR-LIKE PROTEIN 6; 1.
DR PANTHER; PTHR24050; PA14 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF00629; MAM; 1.
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; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..520
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018714182"
FT DOMAIN 92..131
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 172..210
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 217..255
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 369..514
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 312..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 57857 MW; 72F0F2EFFB16A422 CRC64;
MQPFTLVWAL VLVIYVCSGS AEAHRHYRQV LTGNQPGVCR YGTRLECCYG WKKNSKGHCE
AQCEHGCRHG ECVGPNKCKC VPGYTGKTCN QDLNECGLKP RPCEHRCMNT YGSYKCYCLN
GYTLMPDGSC ANSRTCSLAH CQYGCEEVQG EIRCLCPSAG LQLGHDERTC VDIDECVTGK
NLCPFNRQCV NTFGSYYCKC QDGYDLKYVD GKYDCVDVDE CAAGSHKCSH HAVCLNTQGS
YKCKCKSGFR GNGFECSAIP ESQAGPRILG GKQDNEDIKN IIPEPITTPP PGIPQQPFDY
DGEVYIGTQT EERPEAEFNE EEEEEEEEED NQLNPRGDVF LSEDFESVVG PATEIKEIQI
APVQEDFIVD CNFDQGACEW VQEKRDDMDW SVAYHDNGAE YYMAVSGLLG EQKDVAKLKL
LLSDRARKGS FCLTFDYRVV GHNVGTLRVL LDNNAYPVWE QSHTRDQGWQ TELLTVAWKE
EAPQSLIFEA QRGTGVGGEI GLDNVALTSG ACQDDVSPVF
//
