ID A0A3Q3MZB7_9LABR Unreviewed; 1791 AA.
AC A0A3Q3MZB7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Laminin subunit beta-2-like {ECO:0000313|Ensembl:ENSLBEP00000026840.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000026840.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000026840.1}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 56723.ENSLBEP00000026840; -.
DR Ensembl; ENSLBET00000028138.1; ENSLBEP00000026840.1; ENSLBEG00000020337.1.
DR GeneTree; ENSGT00940000167093; -.
DR InParanoid; A0A3Q3MZB7; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 11.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 12.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 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:UP000261660}.
FT DOMAIN 16..254
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 382..441
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 442..492
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 531..796
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 801..852
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 854..893
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 894..942
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 943..1000
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1001..1052
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1068..1107
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1108..1151
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1155..1204
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1772..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1294..1321
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1386..1420
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1504..1531
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1625..1771
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 412..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 464..473
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 476..490
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 801..813
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 803..820
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 822..831
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 869..878
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 913..922
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1025..1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1080..1089
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1108..1120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1110..1127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1129..1138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1155..1167
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1157..1174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1176..1185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1188..1202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1791 AA; 199271 MW; D4E29064622863E5 CRC64;
LSVFGQELPS GPHGCTEGSC YPATGNLLIG RAVNLSASST CGLDGPEHYC IVSHLQGSDK
CFECNSQHHY DPYRHRNSHR IQNVIYLMDH NGENTWWQSV NGEENVSIRL NLEAEFHFTH
LIMKFKTFRP AAMMIERSAD FGRTWRPYRY FASNCTKSFQ GIPSDGLNHI NDVICEERYS
DIEPSTNGEV IYKVLDPAIH VKDPYSFDIQ LLRITNLRIN FTKLNTLGDD LLDRRFDVLQ
KYYYALYELV VRGSCFCYGH ASECAPVPGV DAREKSMQIH GRCVCNHNTE GLNCERCKDF
HNDLPWSPAE AENSHTCRCN CNGHSNQCHF DMAVYLATGN ISGGVCDDCL HNMMGRNCEM
CKPFYHQDPL RDIRDPQVCV ACDCDPVGSL EGGVCDSHTD LDMGMITGQC RCKNNVKGMR
CDDCKEGYYG LSQNDPLGCQ CNCDPRGIIM MGAPCDQISG DCSCKRYVTG RYCNQCLPEY
WGLSNDLTGC RPCDCDFGGA FNNCMMENGQ CDCRRHLIGR QCSEVQPGYF CAPLDYYKYE
AEEATGHSPD DSALPGKVRP QAETDCVQHL NNQLRRHRRH RRITNSQQHR AALRRIRQLQ
QTPDVRTVYR EHTPSHMVSW TGPGFARVKD GAGLVFTIDN IPYAMEYNIM IRYEPESTED
WEAIVSITSV MLPSSLRCGN LLPTEQLYTV TLPHRNYIQM PRPFCFEPSN RYVVSIRFQR
HGVSHRHLTA FILVDSLVLI PNYTELPGFQ GSDPVAEQHR EEMIRYMCLD SFMITPMPAL
AEMCAKLICS ISALIHDGAL CQCDPQGSRS GECDKVGGQC HCKANVMGQR CDQCAPGTYG
FGVNGCTCDC HPEGSLSHQC DPVTGQCHCR QGATGRQCSD CQPGQWGFPS CSPCQCNGHA
DLCDPHTGEC RDCRDYTTGH LCECVDGFFG NPVLVSGEHC RPCPCPGNPG SDHFNGHSCE
ADPTSNQIIC ICKQGYAPRC DQCAPGYYGN PKQPGGQCLP CQCNGNIDTQ DPNSCDPRTG
QCLKCLYHTD GASCAHCQHG YYGNALAHDC RCTCVTAGTI KSACSDGQCH CDRQAGACPC
RENVAGHNCD QCAPNHWNYG QDEGCEPCSC DPQHTLGSHC NMFTGQCHCR PGFGGRQCTE
CEQFHWGDPR VQCQCNCHPL GSEMAQCDRA TGACECREGA AGKRCDECAR GFTGTFPSCV
QCHPCFQLWD DAICQIKRDM DHIQYVIQKI LESGVTPGVG DTRIKELERK LKQIQDLISS
KDSDRVHQLI GQSIDDLAEI ALTDGRLMGI ARELNTTSAE EEALRNTLTD LETELRDINT
TVALKQSLLD NYLTSGFKQF EKVKNYYQQS VEAEQKCNAS VSGPSSPVQQ SKETRAVTEE
LLDLSKDKFL RALAAQNKSL NELQQKTHDL DKKVHHLSNK FQVCGGHSSA DGNCTDSQCG
GAGCRDNQGN RVCGGEGCNG TVSASVAALN HARNVTHSLT AANEELQNVA KKFQDIAALT
QDVKNQAMKT LEKAQKKKDH FENNNKKLKD FIKKIRDFLT EGADPESIEK VALQVLSISL
PFNKTTIDKM IMQIKDSLSN LTNVEGIVNQ TSQHISTAKE LLEKAKDAMR AEGVKDAANN
TKQALDVSET AIEKARAALT EATNNLNSTR NATAEVEERL KQLEEKQMDV MMRLTNLSMG
VEALRNKTEQ NRQMARDAKA QADNATHVAT SLQQSLNDTE KRYHELQMKI DSLGGESGGL
MNINQRAMDI KKEAEDLLNK ASKGMDQLKL EKKFKSNEQR MQRQRTDLDQ L
//
