ID A0A3B5QUN2_XIPMA Unreviewed; 614 AA.
AC A0A3B5QUN2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Multiple EGF like domains 9 {ECO:0000313|Ensembl:ENSXMAP00000034196.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000034196.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000034196.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000034196.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR AlphaFoldDB; A0A3B5QUN2; -.
DR Ensembl; ENSXMAT00000030508.1; ENSXMAP00000034196.1; ENSXMAG00000020951.1.
DR GeneTree; ENSGT00940000167171; -.
DR InParanoid; A0A3B5QUN2; -.
DR OMA; YIGPNCN; -.
DR OrthoDB; 5491831at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 5.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 5.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00180; EGF_Lam; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..614
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017313389"
FT TRANSMEM 527..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..236
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 237..283
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 284..333
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 384..436
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 30..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 210..219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 237..249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 257..266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 303..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 409..418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 614 AA; 64292 MW; 604D211CDE67F23C CRC64;
MSLTSSMMYI SPALLLILYG YIGFSESAPR ISPSDASSIS SRKPGSGGWD AFRTGEPRAA
SPGTRTLSSP PAGITSHPTS PGSPGSEKAT TFQPPTTDPT TTTSRTTATP DAGIISPIKE
QITAPSSRLT LSRKRSTDAQ TSLFSPEKML QTMVSMVSQH TTNDAWAADN ADASVTSVEN
SQEGVCNCSS GTEGISDPDV CNQSTGQCSC LLGYTGLQCE ECEEEYFTNG TSGCLPCSCD
SFGAVSPDCD SSGTCTCKTG VYGPKCDECH PGFFHFSNTG CRLCQCNNHT NYCHPQSGVC
LNCEGNTQGS NCEECKVGFF RRPGAAPTEV CAPCPCSNST STGTCLTDSS GSAVCERCLS
HYSGPHCDQC SPGFYNTSGT CAPCDCSGNA DPLGPAQLCD PKTGSCLRCI NNTSGSRCHE
CASGFVGDAR AHNCTRPKAW VIPAPAEVTT KTPMSGGSSP TSPFTSTTLT STATKGNPVH
RSNDNGGTAL GSSTTTTTTQ ALLTSLSSPT DNTTAALKEV SWTQFKVIIL AVIILVVVLL
LGFVGGVYTY REYQNRKLNA PFWTIELKED NISFSSYHDS IPNADVSGLL EDEATEVAPN
GQLALTTQAN NYKA
//
