ID A0A3Q1FXK0_9TELE Unreviewed; 1113 AA.
AC A0A3Q1FXK0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Laminin subunit beta-4-like {ECO:0000313|Ensembl:ENSAPOP00000023121.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000023121.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000023121.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSAPOT00000012044.1; ENSAPOP00000023121.1; ENSAPOG00000004964.1.
DR GeneTree; ENSGT00940000165244; -.
DR Proteomes; UP000257200; Unplaced.
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 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; 10.
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; 11.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 8.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 21..248
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 376..427
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 451..558
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 614..661
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 662..707
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 708..755
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 815..866
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 867..923
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 924..971
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 972..1018
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 398..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 614..626
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 616..633
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 635..644
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 662..674
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 664..681
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 683..692
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 727..736
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 739..753
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 839..848
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 896..905
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 924..936
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 926..943
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 945..954
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 972..984
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 974..991
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 993..1002
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1113 AA; 124163 MW; 4F6537E99161E7D1 CRC64;
MQHLFSHGTF VLPSDLQDQC PGGSCNPQLG DLMVGRAAQL SASSTCGLDG PQNYCIIGYL
EKCFTCDSRL PYNRYNNPNS HRIENIITTF DPERKMKWWQ SENGVHEVSI QLDLETVFQF
SHLVLTFKSF RPVAMLIERS KDFGRSWKVF RYFADDCSLH FPSVTADPAD SIDDIICDSR
YSGSEPSTDG EVPPGTHTIT QMHTTQALVE EFSTLLSKGA IEPVDPLFRP KGFYSTYFLV
SKKSGGFRPV FFXFFPESRC FFLNPGVFCF QVHGRCVCQH NTAGENCERC LDFHHDSPWR
PGGENTANIC RRCNCHDHSD SCHFDAARFR ATGGVSGGVC DGCLHDRTGP QCEQCRPFLY
QDPQRAREDP HACIPCDCDP AGSQGGGLCD ALSGRCVCKE NVEGERCDRC KRGFFGLRQD
DPAGCQEDGQ CLCFPNMIGR RCSDPAPGYF LPSLNYFLYE AELTAPLPGA PPPSSSSLVS
NGRVVVVRRT RRLARRRIPL EPGHALQIIP RQRSADQPVT WTGLGLVRVV DGAGLRFTVD
NLPSSMEYQL VIRYEPEVSR TSAWSWSWFW SWFWFRSRFR LIKERLTQDN RQQIKEKCYF
MRFLPVLCEM TCSCGCNVIG SRGPYCSKLG GLCECKPNVI GRCCDTCAPL TFGFRSDGCK
RCECDPAGSL SELCDQVRGQ CACRAEVAGR RCDRCQLGFW EFPRCRPCGC NGLSDECDPE
NGECFNCREY STGPSCNRCV EGYHGDPTSG QPCQPCLCPD VWSSRRFFAT SCQYDPQSLS
LTCTCQRGHT GVRCDRCSPG FYGDLTLPDA SCQECSCSNN IDLSDRNACD GRTGECLRCL
HNTMGTHCQT CRPGYYGNAL DRDCKECSCD RRGTQVTQCP LGSPCFCDPS TGQCPCRTGV
MGDLCDECED GYWNLDGASG CQTCSCDPVN SFSNVCNKVT GQCPCRPEFG GRQCDECGEN
HFGNPDLQCV SCDCNLEGTE RPSCDPETGE CICRVGVTGI FCDECAPGYD SAFPACERCH
ACTALWTENV TDVQRAAQRM RTFIPRHDDD EQLAGHHLQR MLEMHSKLDS LSNLTGLSQP
KVEKMQKMFV KIRWVVNVKE SPAVLKHCFP MLK
//
