ID A0A3B4D2F6_PYGNA Unreviewed; 1837 AA.
AC A0A3B4D2F6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Laminin subunit beta 2 {ECO:0000313|Ensembl:ENSPNAP00000018517.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000018517.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000018517.1}
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:PRU00076}.
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DR RefSeq; XP_017537019.1; XM_017681530.1.
DR RefSeq; XP_017537020.1; XM_017681531.1.
DR RefSeq; XP_017537021.1; XM_017681532.1.
DR STRING; 42514.ENSPNAP00000018517; -.
DR Ensembl; ENSPNAT00000027744.1; ENSPNAP00000018517.1; ENSPNAG00000024919.1.
DR Ensembl; ENSPNAT00000039005.1; ENSPNAP00000035165.1; ENSPNAG00000024919.1.
DR GeneID; 108410450; -.
DR CTD; 553337; -.
DR GeneTree; ENSGT00940000167093; -.
DR OMA; EQFCIVS; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd22295; cc_LAMB_C; 1.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF197; LAMININ, BETA 2-LIKE; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 12.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1837
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040590532"
FT DOMAIN 29..268
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 269..332
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 333..395
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 396..455
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 456..507
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 547..811
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 817..864
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 865..910
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 911..960
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 961..1019
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 966..1000
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1020..1071
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1072..1127
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1128..1175
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1176..1225
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1713..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1323..1350
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1391..1443
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1527..1554
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1713..1739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 298..307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 363..372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 426..435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 479..488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 491..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 817..829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 819..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 838..847
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 865..877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 867..884
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 886..895
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 930..939
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 990..999
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1044..1053
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1100..1109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1128..1140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1130..1147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1149..1158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1176..1188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1178..1195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1197..1206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1209..1223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1837 AA; 204494 MW; 115BBE6495378FD7 CRC64;
MMTARCLGLL FLVVHTVAQE LPSGPHGCAG GSCYPATGNL LIGRDINLTA TSTCGLEAPE
QYCIVSHLLE VDKCFKCDSR RPYQPDYHRT SHRVENVIYL KDSKGDLTWW QSVNGEESVS
IRLNLEAEFH FTHLIMKFKT FRPAGMLIER SADFGRSWRP YRYFAYNCSR TFPQIPSRSL
QLIDDVICEE RYSDIEPSTE GEVIYKVLDP SIHVSDPYST NIQDLLRITN LRINFTKLHT
LGDNLLDRRP DVLQKYYYAL YELVVRGSCF CYGHASECVP VQGVDTRVSG MIHGHCVCKH
NTEGLNCERC RDFHHDLPWR PAEADNPHTC RECNCNGHSD KCHFDMAVYL ATGNVSGGVC
DDCLHNTMGR NCETCKPFYY QDPARDIRDP VACVSCDCDP VGSLEGGVCD SHTDLDLGMI
GGQCRCKPNV KGQRCDYCKE GHYGLSQNDP LGCQPCNCDP RGITMVGGPC DPISGDCSCK
RYVTGRYCNQ CIPEFWGLSN DLSGCRPCDC DFGGAYSNKC RMDNGQCDCR PHLISRQCSD
VQPEYFCAAL DFYKYEAEGA VAHSPDDPAL PGNPRPQAVN NCAEHLNNQL RRHKRHRRIA
QQQRAALRRI RQLQQTPDVM TVHRERQPGQ MVTWTGPGFA RVKDGAGLVF TIDNIAYAME
YDIMIRYEPE STEDWEAIVS ITSVLLPTSP RCGNLLPTEQ MYIVILPHHK RYIQMPQPFC
FEPSNRYVVS IRFQRHAVSY RYLTAYILVD SLVLMPKYEE LPGFQGNDPL AQQRREEMVR
YMCVESFMAA PMPPLAEMCI KLICSISSLM HDGALPCHCD PQGSLSAECD KVGGQCHCKP
NVIGRNCNLC APRTYGFGPY GCTACDCHLD GSAGQQCDPS TGQCPCNAGA HGRQCSNCQH
GHWGFPNCRP CQCNGHAESC DPHTGACHEC RDHTAGHQCE RCMDGFYGNP VLGSGEHCRP
CPCPGYLDSG HSNGDSCHMD PASNQIICHC KQGYTGPRCD QCAPGFYGNP EQAGGECRPC
ECNGNIVAED PGSCDQHTGQ CLKCLYNTDG LSCSECKPGY YGNALVRDCR RCTCMTLGTQ
QAYCSDGLCY CDKQTGLCPC RTNVEGRNCD QCASNYWNLG MDRGCEACGC HPQNSLSPHC
NLISGQCHCR PGFGGQQCTE CEPLHWGNPN VQCAECRCDP LGAEALQCDR TTGACLCREG
TSGRHCDECA RGFTGSFPKC VSCHPCFQLW DDIVCQVQRD LDNIRLIIAK ILEMGTVPGV
SDARIRELEK KLAEIQDLLK DGDRDRMYQL ISQAIDDIRA EIAITDGRLM GIEREINGTA
EQDNSLKRNL TSMEQELRDL NDTLAQRRKD LNDYLTAGFA DQFEKVRKYY LQSLEAEQRC
NASVFGPESP VEQSQDTRNR TETLLEQKKD QLLRTVTAQN KSLSELEKKA NDLNNKVHHL
SHKVCGGSGN VGANDTCADN SCGGTGCKDS NGTLLCGGPK CKGTVGDSLR ALQNAHEVTK
NLTAASDDLM NIGKKLQNIA ALVQNVKTQA MNTLEKAQKK KELFERSNKK LKDFIQKIRD
FLTEEGADPE SIEKVAKQVL AIELPVNRTL LDRVVQQIRD NIANLTDVER IFNQTSAHLD
MAKQLLNRAQ NAGAQADRVG DAISKTKEAM NTSQEAIEKA EKAIEMAMEN LDATKNATAM
VEDKLTNLEK NLRNVMSRLA NLSQGVEMLK NKTEQNRQQA QEAKALADNA TQATSELSKE
MSEAESRYKE LKDKVDSLGG AGAGNITQKA IDMKKEAEAL LKKVNKDMEA LKKLERMFLD
NEQRIQKQRD EIAQLETNAT EVRKMIQMKV IGYNTCQ
//