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Database: UniProt
Entry: A0A3B3D254_ORYME
LinkDB: A0A3B3D254_ORYME
Original site: A0A3B3D254_ORYME 
ID   A0A3B3D254_ORYME        Unreviewed;      1788 AA.
AC   A0A3B3D254;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Laminin subunit beta-4-like {ECO:0000313|Ensembl:ENSOMEP00000024212.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000024212.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000024212.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; 30732.ENSOMEP00000024212; -.
DR   PaxDb; 30732-ENSOMEP00000024212; -.
DR   Ensembl; ENSOMET00000010237.1; ENSOMEP00000024212.1; ENSOMEG00000004714.1.
DR   GeneTree; ENSGT00940000165244; -.
DR   OMA; RRCSCHP; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd22301; cc_LAMB4_C; 1.
DR   CDD; cd00055; EGF_Lam; 11.
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; 9.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 12.
DR   PROSITE; PS01248; EGF_LAM_1; 5.
DR   PROSITE; PS50027; EGF_LAM_2; 8.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1788
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017334144"
FT   DOMAIN          28..268
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          399..450
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          451..499
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          539..804
FT                   /note="Laminin IV type B"
FT                   /evidence="ECO:0000259|PROSITE:PS51116"
FT   DOMAIN          810..857
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          858..903
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          904..951
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1012..1063
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1064..1120
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1121..1168
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   COILED          1318..1345
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        421..430
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        471..480
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        483..497
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        810..822
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        812..829
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        831..840
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        858..870
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        860..877
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        879..888
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        923..932
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        935..949
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1036..1045
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1093..1102
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1121..1133
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1123..1140
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1142..1151
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1788 AA;  197807 MW;  5C45F3E9C143A3A7 CRC64;
     MKKMVIFLAV FFPAVHFHSL SDLQDQCPSA PCEPPLGDLM VGRQAQLKAS STCGLKGPEQ
     YCTTGHLQEA RNCFLCDSQL PYSYHSNRNS HWIENIIMSS DPDKNMSWWQ SQNGVHQVSI
     QLDLETVFQF SHLVLTFKSF RPAAMVVERS KDFGQTWKIF RFFADDCALH FPSVLRGPAS
     SIADIICDSR FSGPEPSTGG EVVLQALDPM FEIADPHAAI IQDLISMTNI RLNFTRLLTL
     KDTLPARRQR SPVDNYYYAL FNMVIRGSCF CNGHATQCMP IYREQGNVVT QSGKVHGRCV
     CHHNTAGHNC ERCQEFHHDT PWSPGGETSA RVCRKCNCHG HSEACHFDAA RYQLTGGVSG
     GVCDNCQHYR TGAQCERCQT YMYQDPEKTM DDPRSCIPCD CDPDGSHGGG LCDALTGQCF
     CKENVEGWRC DRCKQGFFGL RRENPSGCYE CHCHTLGSVA SCDPLTGNCK CDSLAYGPHC
     DRCVTGFWGL GNSTIRCSPC DCDIGGAHNT RCSSENGQCH CLPNMIGRTC SEPAHGHFLP
     PLNYFLYEAE LAAPLPEIRL SPSMPTSSSV QSPKVLPPCE QYFKERGFDF SFSSGQIVLV
     QRAHQLRSPH KRQLQNIIPL VPGYASQIIP GQKSSDQKVK STGLGLVRVL EGTGLTFTVD
     NLPSSMKYHL VIHYEQETLS DWLATISIRM LLPGDKGCSK DSIERMLLNL PDTSRAGILD
     SPVCLNAGAL YLVEVLFYSQ PTTEGLHILV DSMGLIPSVE SIQDCSQKTL QPFHCTGLAI
     SPDSQESLPE VCERLIKSLS ARIHYGATAC ECNLTGSLGP ACSKLGGFCE CKPNVIGRCC
     DTCAPLTFGF GSEGCERCEC DPRGSSSKWC DQVEGQCMCY SGVVGRRCDH CKAGFWGFPY
     CRPCECGGRS ETCHGETGAC VNCREHTTGG HCDRCAEGYY GNPISRQPCQ PCLCPGTLRS
     GHFFATSCQQ DSQSLGVSCD CLVGHTGSRC EICLPGFFGD LTAPGFSHCR PCLCNSNTSP
     DDLYPCDRKT GECLHCLHNT SGPQCQACKP GYYGNALTQD CKECSCYRKG TVVSQCPAHG
     PCFCNPRTGQ CPCRRGTEGD LCDRCEDGYW DLDGWGGCQP CSCHPEHSMS NKCDKVTGQC
     HCHPEFGGQQ CNMCGENYFG SPELQCFPCD CHLEGTERPS CDPETGECIC GSGISGILCD
     ECSPGYDATF PACKICHSCA SLWAEEITDV QKAARRMKTF IPQPNGTLQQ TISSQQQRIL
     DGYFTVGSLV KIMLMFLPRL QKLDKLCVQI RMLKDSIDTN TILIDPSALL FIEIHGTKQQ
     SKNLLNNLKD NLIKGKDEER DVKKELLLQI LKHHKSFMLN EEGLRNFSTT LENSMDTRHE
     VLRKLSRCSR IGALAKLEQK VKDLSVVTFN HKASKRPCLK NCSVDGAAPC VLLLGGPDCD
     GGVSISHIAL STLEKAKDQL IGFQAKLQRA EKKIYNALKL AQTIKDHAKT LQTQLISNAV
     TLQRKKTHTR DLFQRAKLLI TDNTVSPDDI KEMATDVLSI HLSLSPDEIW SVINVSNNLT
     SKSGKVQYNL TDLKNQAAVG QGLLHKVQYS RQQTAGMDIK NINIDIFKVH RSNSRTSENL
     TKATGDQNNA DSHMKDVESK LDSIKSKLEK APDLSTEIKN VKDKTEQTNF LVTEATDAAE
     DGFNDIVDAQ GTFRLVMKLF WAFKKETSAL KLAANTPHQL TKIAKGAKDF EKEVEDKFKQ
     TQDVEQRIKW LLNRKKQKEL QLFQLLKIVY SLRQDILSRV VSYSTCSS
//
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