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Database: UniProt
Entry: A0A1S3M9N4_SALSA
LinkDB: A0A1S3M9N4_SALSA
Original site: A0A1S3M9N4_SALSA 
ID   A0A1S3M9N4_SALSA        Unreviewed;      1890 AA.
AC   A0A1S3M9N4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Laminin subunit alpha-4-like isoform X1 {ECO:0000313|RefSeq:XP_013999729.1};
GN   Name=LOC106571319 {ECO:0000313|RefSeq:XP_013999729.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013999729.1};
RN   [1] {ECO:0000313|RefSeq:XP_013999729.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013999729.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   RefSeq; XP_013999729.1; XM_014144254.1.
DR   KEGG; sasa:106571319; -.
DR   OrthoDB; 90222at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa15.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   CDD; cd00055; EGF_Lam; 4.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF00053; Laminin_EGF; 5.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00180; EGF_Lam; 5.
DR   SMART; SM00282; LamG; 5.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 4.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1890
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010215575"
FT   DOMAIN          56..105
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          162..215
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          216..262
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          263..309
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          905..1104
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1116..1293
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1300..1467
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1536..1707
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1714..1887
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          1475..1550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          507..569
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          658..685
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1511..1528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        75..84
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        187..196
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        199..213
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        235..244
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        283..292
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1890 AA;  209709 MW;  D16B9665DD286C20 CRC64;
     MSATKALPCL CLLLSIVLSG IVYPATSIGL HWEQQSVMKV CAQRYFLSNQ KKCLPCNCKG
     HSETCEDITG VCTSCQDHTT GDFCEICEDG YMTDVSNHGH HSCQPCACPL SSPSNNFAEH
     CDRSSNILRC NCQEGYAGHY CERCAPGFYG NPMVIGDSCK SCDCNGNSDP NHIFNECHNV
     TGFCQNCWGD TAGANCERCA PGFYGDAISA KNCRVCECSK CGTTSCDDRT GTCHCKPGVT
     GRLCDQCEEG HTGFNNCQGC HSCDCGPAGL RPTCHPLTHS CQCKPGAGGR YCERCLPDHW
     NYGPSGCQKC DCASSHCDVH TGECLPESYT VNLCNISCDE CIWHLIGDLR PSNKTLDQIK
     VSVLNISTGA AANDRLKYYN YTAQRLKTQF VNWRNKSALM RTQTGQLEEV SAVLLLDMNH
     LAETESVVKS LGDRVDDDTL QSVTLADELT TNLTALNVLI EEMISDWELY SVHQELDPEI
     IRQKTAVAEG MVAWMKKLDL SPQEPIATDE STEAHDLLRR MRQLEKKLIS TDSRVAPVRE
     VLSRFTNKLS EAQEILQKAA NTVEETEDMN KANTVKFQRS EVTSHDPGAK QHELIENYEA
     VNDTLQMAKD LIMDTENTVA EMHLLVQNVT EYHAVIDGAS KGLQEKTEVL PQADRDLVLR
     AQDHAEDLQS QADELEYNLK RSDANGFVQK ALDTANVYNN IVQYIEEANI TGLTTMDLAT
     RAEDTRDGIN TQLGFLKTQS ENVFKESVSL HSEQFEVEAE VLDKMKYIEE TKETMEDYTK
     KLVVVLKDIK GIEPGRTTKR LELTREVAEG TLNRSVEVLQ TITPIHGKVE EWVTNMKNQD
     YSAAAFDRAV VSAGEAVENL SELVPELLDK LRVVEEKNPV NNVTTNIMRI RELIAQARSV
     AKKVQVSMKF SGQSSVQVQP HTNLEDLKTV TTISLFIRVD PDKDPIEDRF IFYLGDRNGR
     KDYMGLAIKN DNLVYVYNLG EEDVEIPLGS KPVSQWPPVF NLIKVERLGR HGKVFLTVPS
     QASTDEQKFI QKGEAFGTDS LFDLDPEDTV FFVGGVPADV RLPPALSLAP FVGCIELASL
     NNDVISMYNF KQTHKMDVVA STPCPRYKLA FSQSRIASYL FDGTGYALIN NMERRGKFGI
     VTRFDIAVRT VANNGILLLM VNGDNFFLLE LKNGFLRLMY DFGFSGGPIV MESNSPKLQI
     NDARYHEVSV IYHYSKKLIL LVDKSHVKSM ENEKKTLPFS DIYIGGAPLH ILLSRPDLSS
     LVGLKGCVKG FQFQKKDFNL LEEPGTIGIS SGCPEEYFMS RKAYFTGESY LGSAAKISPF
     DTFEGGLNFR TLQPTGLLFY HSEGSDEFTI TLENGAVVLN SRGTRVKSQK KQYNDGITHF
     LVASVNNDKY ELVVDDKDKH EKKRPTTAPS ASTVRNFYFG GSPSSSSSIK NFTGCISYAY
     ISRQDRDIEP EDFQKYTENV QTSLQDCPVK RPSAALFSKQ SKNSAKPKKG HTRKVGRDKS
     NLPKGLLGLN SDDQEPRETE ETPCYRSPRP RATHHAHHYG GTANSRQEFT DIPGSLSERS
     HFSLSLKTQS SFGLIFYASD EAEDNFMALF LAHGKLVYTF NLGQQRVKIK SLEKYNDGAW
     HNVIFIRDGN LGRLVIDGLT VLEDRAQGSN VSWHVSSHLY LGGVPPGRAQ KNIQRNSAYS
     FTGCVKNLQL NGQWLSSVSQ TFGVTPCFEG LSEPGTYFSE EGGYVVLDDT FNLGLKFELV
     VEVRPRVASG VLLHVYTAAE EYFTIYIHQG AVVVLVNNGV REFFTQVTPR LGMCDGSWHR
     ITVIRDANVV QLDVDSEVNH VVGPLNPSTQ SARTPVFIGG APESLLPEGI ATRRAYTGCM
     RKLIVNESQV SFSKAALVSG AVSVGSCPAA
//
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