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Database: UniProt
Entry: A0A3B4B0J2_9GOBI
LinkDB: A0A3B4B0J2_9GOBI
Original site: A0A3B4B0J2_9GOBI 
ID   A0A3B4B0J2_9GOBI        Unreviewed;      1367 AA.
AC   A0A3B4B0J2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Laminin, alpha 4 {ECO:0008006|Google:ProtNLM};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000023057.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000023057.1}
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   Ensembl; ENSPMGT00000024564.1; ENSPMGP00000023057.1; ENSPMGG00000006952.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd00055; EGF_Lam; 3.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR15036:SF47; LAMININ SUBUNIT ALPHA-4; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00282; LamG; 5.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE   4: Predicted;
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}.
FT   DOMAIN          84..138
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          139..192
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          423..622
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          634..814
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          821..989
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1040..1220
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1227..1367
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          915..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          989..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..929
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        109..118
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        164..173
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        176..190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1367 AA;  151261 MW;  FB193C7B3850970E CRC64;
     MVYYNTDVIL PGADTAKVCG KGFFLSERGL CLPCNCKGNA DHCQDITGVC INCKNHSTGD
     FCEHCEDGFL LGAGPNGRRS CQPCACPLAC LSSFAVHCDR GTGSLRCKCQ EGYAGHSCER
     CAPGYYGNPM VIGSSCKRCD CSGNSDPNLI FNECHNVTGH CQHCWGNTAG ANCERCAPGF
     YGDAITAKNC RECECESGHC DMHTGECLLE AAISLCNSCD ECTWSLIGDL RISNKTLDQL
     KVAVLNISTG AAANDRIKYY NYTALRLQVV TPHTLLFQQA GSVDTLCIFE TTNTGFVSDL
     CCSDLRESDA NGFVQRAISA ANVYNNIIKY IHDANITSRT TFNLSQKAQE VFLPVRLWDA
     VIYSVKSNHY AYVAVENLNI LVPELLDKLR VVEQKKPVNN VTTNILRIRE LIAQARSVAK
     KVQVSMKFSG QSAVEVHPHT NLDDLKTVTS ISLFIRVDPD KDPIEDRFIL YLGDRNGRKD
     YMGLAIKNDN LVYVYNLGGE DVEIPLGSKP VSQWPAVFNY VKVERLGRHG KVFLTIPSQS
     SSDEQKFIQK GQAPGTDSLF DIDPNDIVFF VGGVPAGVKL PPPLSLAPFV GCIELESINN
     DVISLYNFKE THQMDMVAST PCPRYKLAFS QSRIASYLFD GTGYALINDI ERRGKFGVVT
     RFDISVRTVA NDGVLLLMVN GLKFFLLELK NGYLRLIYDF GFSGGPNRLE EKLPVLQIND
     AKYHEVSVIY HQSKKVILLV DKGHVKSIEN PKTTLPFSHV YIGGAPSNVL KISVYRTELA
     TVVGLKGCVK GFQFQKKDFN LLEEPGTIGI SSGCPEESFM SRKAYFIGES YLGSTAKTSP
     FDSFEGGMNF RTLQPSGLLF YHREGSDEFS IALENGGVIL NNRGTKVKSH KKQYSDGRTH
     FLVASINNQR YSLMIDDKDK QEKKRPPSAS RTSSDSTLKN FYFGGSPHSS LKNFTGCISY
     AYISRLERDI EPEDFQRYPE KVKVSLQECP VRRPPAALQS QNPRGTRGEH SKKHNSDDPN
     TEGGSCSQSP ISRAPQRTFH YGGFSHSRHH YSLPQHALDH RYEWSFCVHR WHLSLSLRTI
     SSFGLMVYVC DMEERSFMAL YLAHGRLELT FSAGGDPVTI SSQNKYNDGK WHNVDLIGDG
     NLGRLIIDGL TLLETRAPKD RGTNSSSQLQ GPLYVGGVPP GKAQRNVPTS SLHSIPGCLR
     NLQLDGEWLP APDSFGVVPC FSGSFEEGTY FSTKGGHVLL DDSFHLGLRF ELQMEVRPRV
     DSGLLLHVRT VEGYFSLFLH QAIVLVNDGT HEFFTKVVPK HSLCTGTWHR ITVIRKANVV
     QLAVDLEVNH VVGPQGPNVN YIGPVWIGGA PSKTIHVHTS FSLATVL
//
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