ID A0A1S3KY36_SALSA Unreviewed; 1629 AA.
AC A0A1S3KY36;
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 gamma-3-like {ECO:0000313|RefSeq:XP_013983602.1};
GN Name=LOC106562972 {ECO:0000313|RefSeq:XP_013983602.1};
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_013983602.1};
RN [1] {ECO:0000313|RefSeq:XP_013983602.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013983602.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
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_013983602.1; XM_014128127.1.
DR STRING; 8030.ENSSSAP00000093621; -.
DR PaxDb; 8030-ENSSSAP00000093621; -.
DR GeneID; 106562972; -.
DR KEGG; sasa:106562972; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
DR Bgee; ENSSSAG00000070439; Expressed in nose and 7 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 9.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF240; LAMININ SUBUNIT GAMMA-3; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 10.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 8.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Secreted {ECO:0000256|ARBA:ARBA00022869}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1629
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010342650"
FT DOMAIN 35..271
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 328..383
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 384..430
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 431..480
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 507..682
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 717..764
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 820..875
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 876..926
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 927..974
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 975..1022
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1290..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1230..1268
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1578..1612
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 356..365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 384..396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 404..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 451..460
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 734..743
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 844..853
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 899..908
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 927..939
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 929..946
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 948..957
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 975..987
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 995..1004
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1629 AA; 178997 MW; 6556DD26F43BBAE3 CRC64;
MDIPLTTPLL LALLLCSLSF VHGAMDSCYD DDEGVPSRCM PKFENAAFNR TIMASNVCGS
PPEDYCMQTS STRSCHHCSV SDMGLSHNAS LLTDFHTDEE PTWWQSQSMF YRVQHPNSVN
LTLRLGKAFE ITYVRLKFYT SRPESFAIYK RTNQDGPWMP YQYYSASCSK TYGKNAKGYI
RPGDDERMAL CTDEFSDISP LTGGNVAFST LEGRPSAYNF DQSAVLQEWV TATDLLISLD
RLNTFGDEFF KDAKVLRSYF YAISDFSVGA RCKCNGHGSE CVLDEQGALV CDCQHHTAGV
DCQKCHPFYQ DRPWARATGD SANQCMKCNC SGRADACVFD AEQYRSTGSG GRCVDCRDHT
DGPHCERCKE KHYRRSPQDL CRPCDCNTIG SVSLQCGGEG MCTCRPSVTG EKCDTCQPGF
HSLSPGGCRS CDCETRGSVG ICSTLDGGCH CKDNVEGQAC DRCKPGSFNL QENNPAGCTS
CFCFGHSLAC RSSNHHAAIN ITSDFLEDPD RWSGQFSGGQ EYPLLWKEGE VYLLPLSEDD
LGFYRAPEKF LGNHLLSYGQ LLSLTFTAEA QCLLPHSVTV LLEGSGITLS ADLSPQPGLV
HQPGLAPQHT FTLRLHKEET RLRPFLSAFE FQSLLFNLTA FRISNAGGHN YTSQLSGVTL
ASAAHSSSPV TSSTPPAPWV EVCTCPPGFG GQFCELCAPG YTREVPNRGP LSPCVPCTCH
QHGPCHPETG VCECADFTTG PTCERCLDGY YGNALIGTTN DCRTCPCPDR TSCAQMMEIG
DVVCTNCPSG QRGTRCELCE DGFHGDPLGR SGLVQQCERC DCNGNVDPNA LGVCDHMTGR
CFKCLGHTEG DHCQRCQRGY YGDAMDRTMA GKCKPCDCSP AGTSGLLEDC DPQTGSCQCL
SHVTGGDCGQ CSVGFFNLQP GVGCERCNCN PIGSSSAACH PITGQCVCQP GLEGRLCSTC
RMGFFGFSSR GCRACNCDPM GSSSMQCHTN GTCPCRQGFV GYKCDQCELN YFHNRATHQC
EECPICYGLV KEQAGKLKAR LQDLEKLLAR FDCRSGYGRQ HHVREYHVRQ HHERGHQGED
SLPNALEDFL AIQEAKEAFV KEFALLEMST HTLSAQLHTV TTAMNCSASM EEEQEEGWRT
LCRTLADSVS VVRSARTQLM QATLDLDNMV IPFKVTPVPN RWNSAVNESE ILMKSHTEMA
GHIESIATKA FMASNQTYSL LMDLLEDNSI EEYISNLTEQ MADMQQIKEN LTAQVNETLA
NQLSLEEESA EIMVAFVNLT SSILELSKNF PNPTSGTNQL DPSLRSGANQ TEGVELSNRT
SELAFHVQSK EELASKIKEE MEPRIQTAHN NIAAVQDMHK LTVQAQGSKV IALSSVVTGK
EVESEAITLW RELEDMQREW PQRQAQTKAA LKRERLLREK ILEDVSKKVN QTKRVLRPAL
ESATLSNATA QQAKHTANAL SKEAKATLTQ GKHTRTLSAQ LSSSVDITLQ QLAEQENHTV
HAQTQLNAEP VESLASVKVN IQTAKLQLEA YSLTLTQLVS KIDGSMALER FERILSETAM
RLSVLRGSVE SPALNGKIQT LRSAAQDQES QLTHLEQDLQ EIRQERDSLK DIALHLPQTC
PQASGIEGH
//
