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
//