ID I3JZJ7_ORENI Unreviewed; 1789 AA.
AC I3JZJ7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Laminin subunit alpha 4 {ECO:0000313|Ensembl:ENSONIP00000014292.2};
GN Name=lama4 {ECO:0000313|Ensembl:ENSONIP00000014292.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000014292.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000014292.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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; 8128.ENSONIP00000027809; -.
DR Ensembl; ENSONIT00000014303.2; ENSONIP00000014292.2; ENSONIG00000011356.2.
DR eggNOG; KOG1836; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000165424; -.
DR HOGENOM; CLU_002814_0_0_1; -.
DR TreeFam; TF335359; -.
DR Proteomes; UP000005207; Linkage group LG15.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 4.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
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; 5.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00180; EGF_Lam; 5.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 154..207
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 208..254
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 255..301
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 806..1005
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1017..1194
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1201..1369
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1436..1607
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1614..1786
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1383..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 582..609
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 666..693
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1383..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 179..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 191..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 227..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 275..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1789 AA; 198766 MW; 00DF099B15E790A0 CRC64;
CYISNQVSYC ALFFFYKFLL YRKLTFLFPL QVCGRGFFLS EQSECLPCNC KGHADYCEDI
TGICINCKDH SMGDFCEMCE DGYILTPGLG GRHTCQPCAC PLPIPSNNFA VHCDKGGATL
RCKCQEGYAG NYCERCAPGY YGSPMTTGSS CKRCDCNGNT DPNLIFNECH NVTGHCQHCW
GNTAGANCER CAPGFYGDAI SAKDCRECKC DKCGTSSCDD RTGVCHCKPG VTGRLCDQCE
EGYSGFSSCQ GCRRCDCGPA SLRSTCHPLT HSCPCRPGAG GRYCERCLPG YWNYSPSGCQ
KCDCESGFCD MHTGRCLAEP STVNLCNITC DQCIWHLIKD MENSNKTLDQ LKVGVLNITT
GAAANDRVKY YNYTAHQLQV HAHLHLNWVL MLHVHTEMIH DWEVYSIQQE VDPEVVRKNT
EDAKEIVALM RKIDLSPGEP IATGESTEAH DLLGRIRQLE KKLMITNSRL PSVREILSRF
SGRLSEAQGF LVKADSNVHE TENKNRASVL KFQRHEAKLQ RLMEDHDTVN DTLEAARDFI
AQTERTVAEV DNVTEYHAAI DGASQKLTEK TERLSLVDRD LVQKADKHAE GLERQANELE
EDLRKSDANG FVQRAITAAN VYNNIVKYVD DANITSLTTF NLSERAEDVC QIMQFCELKH
EVADKLKYIE ETKETMENNM KKLSEIVQDI SELQTDRTPQ RLEFTSEVAS ETLNRSAEVL
QSITPISSKV EEWNNNMKNN EYSTAAYEQA VASAGEAVEN LNLLVPTLLD KLKLVEDKKP
VNNVTTNIMR IRELIAQARS VAKKVQVSMK FNGQSSVEVH PHSNLEELKT MTSISLFMRV
DPDKDPIEDR IILYLGDRNG VRDYMGLATK NDILVFFYKL GAEDIEIPLS SKPVSQWPAV
FNYVKIERLG RHGKVFLTVP SQSSTDEQKF IQKGEAPGTE SLFDIDPQDL VFFVGGVPPD
VKLPPPLDLA PFVGCIELSS LNNDVISLYN FKQTHKINLT TSPPCPRYKL AFSQSRIASY
LFDGKGYALI SNIERRGKFT VVTRFDISVR TIASDGVLFL MANEDKFFLL ELKNGILRLM
YDFGFSNGPK LLENNLAKLQ INDAKYHEVS VIYHQSKKVI LLVDKSHVKS MENPKTTLPF
ADIYIGGAPS SILKSRPELS SVVGLKGCVK GFQFQKKDFN LLEEPGTIGI SSGCPEESFM
SRKAYFSGKS YLGSTAKISP FDNFEGGLNF RTLQPSGLLF YHNEGSDEFS ISLENGAVVL
NNRGVKVKSH KKQYNDGRSH FLLASVNNQK YSLLVDDEDK QLKKRPASAV GSSYDSDVKT
FYYGGSPSST SKNFTGCISY AYINRLDLDI EPEDFKRYPE KVQISLEGCP VHQPPAALLS
RHRANTSGTK QSQKVTRDKS SLPPGLTELG SDDQESAEPN IKSCFLSSSP KSIHHAFRFG
SIANSRQHYA DFPDSLSQRS HFSLSMKTHS SFGLIFYVSD AQEDNFMALF LAHGKLLYTF
NVGDQRVKIK SEDKYNDGSW HSVIFIRDGN VGRLIVDGLT MLEDSIQGNN VSWHISGPLY
VGGVPPGRAQ KNIQRNSAYS FTGCIKNLQL DGKQLSSVAD TFGVTPCFDG VSEGGTYFSE
EGGYIVLDDS FNLGLRFELV MEVRPRVASG VLLHVHSADD YFTVYIHQGA VVVLVNDGTR
EFFTKMSPKQ GVCSGSWHKI TVIRDANVVQ LDVDSEINHV VGPLSPSSTD SRKPVFIGGT
PDGFLPESAA TRKAYVGCMR NLTINNSQVN FSKAVLVSGA VSVGTCPAS
//
