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Database: UniProt
Entry: A0A3Q1II53_ANATE
LinkDB: A0A3Q1II53_ANATE
Original site: A0A3Q1II53_ANATE 
ID   A0A3Q1II53_ANATE        Unreviewed;      1546 AA.
AC   A0A3Q1II53;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Laminin, gamma 3 {ECO:0000313|Ensembl:ENSATEP00000017343.1};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000017343.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000017343.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
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; ENSATET00000017635.2; ENSATEP00000017343.1; ENSATEG00000011971.2.
DR   GeneTree; ENSGT00940000166104; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
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   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF240; LAMININ SUBUNIT GAMMA-3; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 11.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00180; EGF_Lam; 11.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 10.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 7.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Secreted {ECO:0000256|ARBA:ARBA00022869}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1546
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018531255"
FT   DOMAIN          39..276
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          389..435
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          436..485
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          512..682
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          717..764
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          820..875
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          876..926
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          927..974
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          975..1022
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   COILED          1514..1541
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        389..401
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        409..418
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        456..465
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        734..743
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        844..853
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        899..908
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        927..939
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        929..946
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        948..957
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        975..987
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        995..1004
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1546 AA;  171015 MW;  CD8F0455E07FD1A2 CRC64;
     MDTPFAVSPL LFALLLSLHL HHHLLVWAAM DSCYDDEGAP SRCMPKFENI AFNRTVEVSN
     VCGSPPEDYC MQTGSTRSCH YCDASDTDLS HNASLLTDFH RNEEPTWWQS QSMYYGIQHP
     NSVNLTLHLG KAFEITYIRL KFYTSRPESF AIYKRTEEDG PWVPYQYYSA SCKKTYRKEA
     KGYIRPGDDD ERTALCTDEF SDISPLTGGN VAFSTLEGRP SAYNFDQSVL LQEWVTATDL
     LISLDRLNTF GDEFFKDAKV LRSYFYAISD FSVGGRCKCN GHASECVEGE HGGLVCSCQH
     HTVGADCQRC HPFYQDRPWA RATGDSANEC LKCNCSGRSD ECVFDMEQYR STGSGGRCVS
     CRDNTDGPHC ERCRENHYRR SPEEPCLPCN CNIYGSVSLQ CDVEGRCACR VGVTGEKCDT
     CRAGFHSLGP GGCRPCECDS SGSVDDCSPL DGRCHCRPNV EGQSCDRCKP GFFNLQQVNP
     AGCQPCFCFG HSLACSSSSH CAAVNITSDF TEGQDGWLGE FSGGQQDHLQ WKEGEVYLLP
     LSEEDTGFYK APEKFLGHQV YSYGQPLFIT FTSETPELLP NHITVLLQGS GITLSADLSP
     QTVFDHDPGL TPRHSFIVRY KDTRFNPSLS AFAFQHLLYN LTSMRISNAG GHNYTSQLAG
     VTLTSAVISS SPANHPAPWV ETCSCPLGFA GQFCEQCAPG FTRKVPGRGP LSACVPCNCH
     QHGSCHPETG VCECSDFTTG MTCEHCLDGY YGNALIGTPA DCQPCPCPDR SSCAQIVETG
     QVVCTNCPTG QTGMRCQMCE DGYYGDPLGQ SGAVQPCERC DCNGNVDFNA LGICDHITGR
     CLKCLGYTEG DHCQYCQQGF YGNALNQTAG QKCKPCSCNP AGTSGHVNDC HPQTGNCQCL
     RHVTGRDCSH CEAGFFNLQP GVGCERCKCN PIGSASPACH PVTGQCVCHA GVEGTLCDSC
     RVGFFGFSSR GCRACNCDPM GSISMQCHSN GTCQCRQGFV GYKCDKCELN YFHNRATHQC
     EECPVCYGLA EKLRTRLQDL EKLLAHFDCR GRFGKEHHLL KYHMARLYEH EHQREDSLPN
     ALEDFLAFQE AREAFIKQFS LLEASAGTLL AQLYGITNAL NCSISMTEKE GKEKDEGSRG
     VCQTFTDTVF KIRASQKQLK QATVDLDNMI IPFEVVSGPN KWNIMVNDSQ FLMKSHREMA
     NDIEAIASRA VRASNQTLSF LMDLLQDNST EEYISNLTEQ ITQMQQQKEN LTVQVNDTVA
     TQLDLEEEVT GLKLALGNIT SSLHQLALTD ATPSPQPNQT HPTNHTTEVS LDTCEVKLEL
     LNNDPSEFNL FIILKNLHLT IYFCPNLHLD MVKEWPRQQA QIKAAIKKER PLEEKVLGDV
     RKKVSQIQKM LKPALENSTL SNTTKEAEQA AHAVAKESKA ILTQAKHTRT ASAHLSTHID
     SALQLLTEQE MVTDTPASSF SICHLSFMFG PDGNVPLERF DRILNETARR LSMLRGSVES
     PTLGSKIQKL HLAAKEQHSR LSLIEQDLQE ITEERDSLRD IALNLP
//
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