ID A0A1S3I6T8_LINUN Unreviewed; 1530 AA.
AC A0A1S3I6T8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Laminin subunit beta-1-like {ECO:0000313|RefSeq:XP_013393995.1};
GN Name=LOC106161546 {ECO:0000313|RefSeq:XP_013393995.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013393995.1};
RN [1] {ECO:0000313|RefSeq:XP_013393995.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013393995.1};
RG RefSeq;
RL Submitted (NOV-2023) 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_013393995.1; XM_013538541.1.
DR STRING; 7574.A0A1S3I6T8; -.
DR EnsemblMetazoa; XM_013538541.1; XP_013393995.1; LOC106161546.
DR GeneID; 106161546; -.
DR KEGG; lak:106161546; -.
DR InParanoid; A0A1S3I6T8; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR CDD; cd22302; cc_DmLAMB1-like_C; 1.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 1.20.1170.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 12.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF375; LAMININ SUBUNIT BETA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 13.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS51116; LAMININ_IVB; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 38..100
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 101..163
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 164..223
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 224..274
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 314..521
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 527..574
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 575..620
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 621..670
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 729..780
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 781..831
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 832..879
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 880..926
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1068..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 961..1068
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1116..1143
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1188..1250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1336..1454
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 66..75
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 131..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 194..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 246..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 258..272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 527..539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 529..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 548..557
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 575..587
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 577..594
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 596..605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 640..649
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 753..762
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 804..813
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 832..844
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 834..851
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 853..862
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 880..892
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 882..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 901..910
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1530 AA; 168364 MW; FD9D4CC01673797D CRC64;
MAKQTSFFER SDDLLDSRPE IKEKYYYSIY EMVVRGSCSC YGHASRCLPL PGLPNRSDMV
HGRCECTHNT KGLNCEQCEA FYNDLPWRPA RGNQSNECKK CECNNHASRC HFDPAVYEAT
GRVSGGVCDD CQHNTMGRNC QECKPFYYQD PTKDIRHPEV CKPCDCDPKG SENSGECESR
SDPEHNLVAG RCFCKRFVDG PRCDTCKNGY WNLREESIDG CEPCECNTYG TVGNFGCNKI
TGVCTCKRFV TGRNCDQCLA GYWGLGPDVD GCKACDCDFG GALNNMCEQT TGQCACRQNI
IGRRCERPRP GYFITNLDYL VYEGEFARGT GNYQVVIREP VAGRPTTWTG PGFMRVSEGD
SLVFTVDNLP SSMEYDIVIR YEPQMPDRWD DVRVTVERPG RVDQNSVCAN SIPQDDFKAT
SLPAGIRYYT VSPPSCLETG VSYTIKLEFN RYKSDRATPD ATALIDSIVL VPRINSIPGT
PQEITTDFER YRCREDQLTA ARPDLAEVCK KYLFSLGAII HQQALDCECD PTGSVSAVCD
PSGGQCQCKP NVIGRRCDKC APGTYGFGPQ GCLACNCNAL GSRDNFCDVT SGQCLCIPNA
YGRQCDQCQR GYYNFPNCRL CQCNGHADTC EDTTGRCIGC RDYTAGDNCE LCVRGYYGDP
RLGANIPCRA CPCPGGQGSG FQHADTCSLT REQNVRCDCR PGYTGDRCDR CADNFYGNPV
VPGGECRACF CNNNIDPDVP GSCDPVTGEC LKCLYQTEGY SCERCKEGYY GDATRQTCQA
CVCNILGTNR SMGACDIVTG QCPCLPNVIG RACDRCAPNH WKLASGTGCE ACNCDPDGSL
STQCNEFDGQ CECKPGRGGL TCGECEAFYW GNPNIACYPC DCNREGSASL QCDRRTGQCE
CLEGVAGHKC DRCERGTTGQ LPNCVPCGEC FDNWDKIIQD LAGRTRLLIQ EANEIKIQGV
SKAYEQVFRE MESKLDQVRQ LIENANVSVA DIEGLKLKLE QLRTQLDGQA NSVQGVEDGV
KEAGREILKT ENSIQVLRLG INGLRQAADE LKKEAEELKE QNVQGAFESL QSSQKRSEAA
QKTVDDTDDT VAQSKQTRER AEQFMADNQA EFQRKTQENE DAIEDVQTDI ELLENQLADV
NNMVCDGRGT PCDVLCGGGG CGKCGIIGGG QSCDAGAVTK ANNSLSLAKQ TEDTLAERSK
NLQDLLGEVE AVEADASVAK SEVQAAFDKA EQAKNMSESS RTELQKLLES IAEFLTKGGA
RPEDIRQVAE EVLAMSISLT PEEIENLAAE INKTVIGLTN IDEILDATRS RNETAHKLQE
EAKKASADAA TILDTARKVS DRLDLAEEAQ DKAQKAIDQA NENIKEAETH LTQVESETDA
ALGKANASLE AVQNLTTKLE DVKKKYVQNE LSVQRAKGEA DGAMKMANKA ESDAADLETK
YQDASAQLEA KYNMTKDAKE RAVQLKNNAT TLAQSTQFKL YQLRTMERDF MEREKSLTEL
SGEIEALLAR MKLLTQEIQE KSDFYRDCQP
//
