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Entry: A0A1S3PBN8_SALSA
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ID   A0A1S3PBN8_SALSA        Unreviewed;      1740 AA.
AC   A0A1S3PBN8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 2.
DT   28-JAN-2026, entry version 44.
DE   SubName: Full=Laminin subunit alpha-3 {ECO:0000313|RefSeq:XP_014025050.2};
GN   Name=lama3 {ECO:0000313|RefSeq:XP_014025050.2};
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:UP001652741, ECO:0000313|RefSeq:XP_014025050.2};
RN   [1] {ECO:0000313|RefSeq:XP_014025050.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) 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   RefSeq; XP_014025050.2; XM_014169575.2.
DR   STRING; 8030.ENSSSAP00000042730; -.
DR   PaxDb; 8030-ENSSSAP00000042730; -.
DR   GeneID; 106584357; -.
DR   KEGG; sasa:106584357; -.
DR   Proteomes; UP001652741; Chromosome ssa23.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-ARBA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004435; F:phosphatidylinositol-4,5-bisphosphate phospholipase C activity; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; 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; 1.
DR   CDD; cd00110; LamG; 4.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR050372; Neurexin-related_CASP.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR15036:SF67; LAMININ SUBUNIT ALPHA-LIKE PROTEIN; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF00053; EGF_laminin; 2.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00282; LamG; 5.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP001652741};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1740
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5045664830"
FT   DOMAIN          103..149
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          150..204
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1019..1182
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1189..1346
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1199..1248
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          1388..1558
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1564..1737
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          652..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        122..131
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        175..184
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1740 AA;  192813 MW;  9C9C4FBDF9C2FE59 CRC64;
     MKMTQGTVCW FGGVWGLLLW CALFGPCTDG QSAPQRHPNG RYDYLSQNHQ SGKDPWHKGH
     PRIPRKYCDT SFNNQSAGAI TQRCGTGYYR ERTGPHRGQC VPCNCNSLSN ECDEQTGRCL
     NCQYNTDGDR CERCKEGYYG NAAQKTCRGC PCPFRANNFA VACLDIGANE IECLCKPGYT
     GTRCERCAPD YYGNPMIYGG RCQRCHCDAT STCDHLTGKC KKPDDPGTND QCIECDSCTQ
     ALLNDLENMD DGLELLRQQL QGIAYNSSPA NLNQLEGAIN ETKALVGRYS TIVDAQGPKV
     NLLEAEVMSL DQDISLLEDK ASYTLSDAEN VLVKVIQTKQ RAEDFIPKAQ DLLMNIEDLL
     RQLSEANSSV NNITVGVEEV ARMMKVVQRM VKEMRQLGCS NQTEKAAREQ EGAHKLLDFI
     KNNMSAPLDD NQAVANETAQ SLMTSVSALS DLAVAVAEAD NTVNRTRSLN FNSTDFLRIL
     TQLSGELERK RDSVLPEMNM TKDKLKNITG LLEMMKEMKK EYEHLAAEID GAKPNLTKRL
     NDIAKAKQKE GIVVMAEEHA EELNRLAMEL QMAVHNATNS SDLQHASEST GAYSSIIKAI
     EEAEMAANQS KEASDKALKD VEEQGLTNRS EELKHNASSL LTEALNAEKD LRETSAKVDN
     HKQRVGQTKN KRKMLRKDAL AVTENLKEIQ RDDIGKLIDS AKATVNAANN TVNDVTDRLN
     DISLAHIMLP NVSSNIGSVL DEVGNELKKL NETWPTLEDT LSRVKNLCSQ ASPSVSMTDS
     IRRIKDVIEE ARDIVKRLSI GMTFNGKGHI ELRPPTNVED LKAFTAAELL LNLQETKPTR
     GDRSRRRRQN TQDDRNLFVL YLGNKDSSKD FIGMAVKNNT LRCVYKLGGV IHELNTDHIT
     RAKVNSTVFD KVVFNRVYQD AELSVTHRFP SQPVDVSKES NRPNTTVGLL NLDTNSVVFY
     VGGYPDAFTP PVELRYPKYC GAIKLSTING QFFSLYNFKN AINVDKQSYI KVSVSLQSTV
     PYYFDGTGYG LVTAIKEIKT PKRGVLKFHT NSQVENAILF YKGNEDSYTS VTVERGYVVV
     QGRQGTQVLN AKSTRKVSLN NEQFVIVMDT TFKVHVTGVQ TEIIKIDNIM ESLKHFYIGG
     LPASLRKRDN VTTPPFRGCI DNVILQSKEI EFNTTIGVSV GCPTSLLGVR EATFHPGGSL
     SVDPQDFWTN PVAMVSLGFR TMENKGVLLR TSEERHGYQL SLVDGYVMFY FDENALKSTK
     TYNDGRWHYL TALRNGTQLE LRVDNGDLGQ HQTTPQVKPN EQQVVLGGET FRGCLANLHI
     RRPEESFIPA DFSSFTQKGD VILGMCRLQP PPQAIWEPAG LQERPKKSKP RSGAVHTECR
     LPKVSDPQAY QLTGAASWLS YIIAPEELNF RPHFSLEIRT RSSAGLLLHV SGNGDISQVS
     LYMTNGKIKL SLGKDRVIHN KNKSNDGRWH TVMVSVEKNT FHLVVDGFRV PDGILPAEEG
     SSLALQNPVY LGSDPASKTS WAQGDSLPKK SVIGCIRHFK VYNVLVGEPA ANHGAPPCFD
     GATEAGAYFA GTGHVVLDKF FTVGSRFELT FEARPRNTTG LLFHARGRHR NSLSVFMRKN
     KVEVHVNDGL GDYSASVTPQ QNLCDGTFHV IAVSKQNNVV QLNVDSESQR TVGPSHSSYT
     MTKDSLYIGG MSGTSKHKGV PISSSFVGCL RHIKVNKKPV VFKTASSVVG PVNINECPAD
//
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