ID A0A315VSJ2_GAMAF Unreviewed; 1135 AA.
AC A0A315VSJ2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 08-OCT-2025, entry version 24.
DE RecName: Full=Laminin G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CCH79_00013751 {ECO:0000313|EMBL:PWA26278.1};
OS Gambusia affinis (Western mosquitofish) (Heterandria affinis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Gambusia.
OX NCBI_TaxID=33528 {ECO:0000313|EMBL:PWA26278.1, ECO:0000313|Proteomes:UP000250572};
RN [1] {ECO:0000313|EMBL:PWA26278.1, ECO:0000313|Proteomes:UP000250572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE01/NJP1002.9 {ECO:0000313|EMBL:PWA26278.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PWA26278.1};
RX PubMed=29703783;
RA Hoffberg S.L., Troendle N.J., Glenn T.C., Mahmud O., Louha S., Chalopin D.,
RA Bennetzen J.L., Mauricio R.;
RT "A High-Quality Reference Genome for the Invasive Mosquitofish Gambusia
RT affinis Using a Chicago Library.";
RL G3 (Bethesda) 8:1855-1861(2018).
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:PWA26278.1}.
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DR EMBL; NHOQ01001193; PWA26278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A315VSJ2; -.
DR Proteomes; UP000250572; Unassembled WGS sequence.
DR GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000250572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1135
FT /note="Laminin G domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016465685"
FT DOMAIN 114..303
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 163..302
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 84..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..416
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..451
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..913
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 119656 MW; FF53C21B5FADC13C CRC64;
MRSWFKALPL LTLWVVYSEA WFWSWSETGT TLAPGLELEG SGIATGSGEP PSESSTTAGA
EITDEGHVLQ TVGQTWDETT EGPRVTTVVP STGRGEGQTT AGTTSRRSKP EDSGVSLLQL
IGDPPPEKIL EVDGPDNSPA YLFGPESATG QLARAHFPNP FYRNFALIFS LKPTSDDGGI
IFSITDSSQQ IMHLGVKLSA VQGSKQNVVL FYSEAGARQS KEAARFHVPS MTNAWNRFAV
AVKDDKAMLY LNCDVEPQVM LMARSARELV LESGSGVFVG QAGGEHPDKF KGAISELRVV
GDPSAAARFC EEDDDSDMAS GEGSGYGETR RPKPFSEKPQ QTGPVGPKGD RGDPGSPGYG
LKGEKGEPGL MIGPDGNPLY LGGLTGTKTA VESLPPMQQP PLERTVQRAQ AGAAAAKGEK
GDRGDRGEKG DQGPTGPKGD TGSGSQGGIR GLKGEPGEKG AKVLDIRVQR VNQALPDHQG
PLDLLDPQHS IQLMGRLFRR FLGRADRLDR QVLRGHPEKM ENQVTPVKME KLGLRDLQGF
QELRVTQELK ERRATVERAS PAPEDPQGLQ DRRTFEDMEA SGFPDMVSVR GLPGPPGPPG
PPGPPGLNSA STSVNSGAVG PPGKDGAPGQ PGLPGLPGAD GLPGAPGPRG EKGDSGDLGL
PGAIGQKGNL VYRDLQESLD WLVCQDPWDQ LVLLDHLGLQ DQDDMEDSSG IFTNGLPGVR
GPEGIQGKPG FPGTEGPKGE QGLAGRDGLP GLDGFPGPPV RKTERYVKTV QHRMGVAGPP
GPPGPPGPPG PAIALDRFNK KESVATVDLL GSQNELKGDQ GDPGVKGEKG EPGGGYYDPR
FGGPVGPPGP PGNPGLPVSS EGAAQLQSST VGPKGESIAG PPGPPGPSGP PGVGYDGRPG
PAGPPGPPGP PGNPSFSGTY RPNYRKKLSV SFSEVFVSFP SVVLGAAPPQ ARRGTDVFTN
FCLCFDLKLS AFLDLLVRQA HLEALVTVLR SYDIMIATAR QQPEGNLIYI LDKADLYLRV
RDGLQQVLVR LHTFSFHFHE PLGDYRTFFG DLGNEVAEVQ PPPVVVYPHT PERTSNNGAG
HYSQSSVVIR PAEPPLRQPS TPVAPAADSS ESGVIATIKT HYCSINMTKQ KPFFP
//
