ID A0A087RKP3_APTFO Unreviewed; 1729 AA.
AC A0A087RKP3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Laminin subunit beta-1 {ECO:0000313|EMBL:KFM14047.1};
DE Flags: Fragment;
GN ORFNames=AS27_01684 {ECO:0000313|EMBL:KFM14047.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM14047.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM14047.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM14047.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; KL226413; KFM14047.1; -; Genomic_DNA.
DR STRING; 9233.A0A087RKP3; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR CDD; cd22300; cc_LAMB1_C; 1.
DR CDD; cd00055; EGF_Lam; 12.
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; 2.
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; 13.
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; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053286}.
FT DOMAIN 1..204
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 205..268
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 269..331
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 332..391
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 392..443
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 483..709
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 715..762
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 763..808
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 809..858
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 859..917
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 918..969
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 970..1031
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1075..1121
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1296..1323
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1394..1449
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1504..1717
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 234..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 299..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 362..371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 415..424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 427..441
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 715..727
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 717..734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 736..745
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 763..775
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 765..782
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 784..793
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 828..837
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 888..897
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 942..951
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 970..982
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 999..1008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1075..1087
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1077..1094
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1096..1105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM14047.1"
FT NON_TER 1729
FT /evidence="ECO:0000313|EMBL:KFM14047.1"
SQ SEQUENCE 1729 AA; 191154 MW; D8DB877FE9D9D516 CRC64;
IILLFQEDKK CFVCDSEDPF HDTLNPDSHR IENVVTTFAP NRLKLWWQSE NAFQIIHVFC
NRLGSIHTEK FLAHKTFRPA AMLIERSSDF GKTWQVYRYF AYDCESSFPG ISTGPMKKVD
DIICDSRYSD IEPSTEGEVI YRVLDPAFRI EDPYSPRIQN LLKITNLRVK FIKLHTLGDN
LLDSRMEIRE KYYYAIYDMV VRGNCFCYGH ASECAPVDGF NEEVEGMVHG HCMCRHNTKG
LNCEQCLDFY HDLPWRPAEG RNSNACKKCN CNGHSSQCHF DMAVYVTTGN TSGGVCDDCQ
HNTIGRNCEQ CKPFYFQHPE RDLRDPDVCE PCNCDPAGSQ NGGICDRYTD FSTGLIAGQC
RCKLFVEGER CDLCKEGFYG LSADDPAGCQ SCACNPLGTH PGGNPCDSET GNCYCKRLVT
GKQCNHCLPE HWGLSNDMDG CRPCDCDQGG ALNNNCSSQS GQCECRPHMF GRQCNQVEPG
YYFISLDHYI YEAEEASLGP GVNIIERQYT PDRTPSWTGI GFVRVPEGAY LEFYIDNIPY
SMEYDILVRY EPQVGLLFSP QLPDQWEKAV ISVSRPGKIP TGSRCGNTVP DDDNQVVSLS
PGSRYVVLPR PVCFEKGLNY TIRLELPQYS SVDTETESPY TLIDSLVLMP YCKSLDIFTV
GGSGEDVVTN SAWETFQRYR CLENSRSVVK TPMTDVCRNI IFSISALLHE TALSCQCDPQ
GSLSSVCDPS GGQCQCRPNV VGRQCDRCAP GTFGFGPSGC RPCECHVRGS YTTFCDAETG
QCHCFPGVYG RQCDRCLPGF WGFPSCQPCH CNGHADDCSP YTGECLSCRD HTAGHNCERC
QAGYYGDPIL GSGDHCRPCP CPDGPESGRQ FASGCYQDPV TLQVVCVCSV GYIGSRCDEC
ASGFFGSPDE VGGACQPCQC NNNIDATDPE ACNKKTGTCV KCLYHTEGEN CHLCKQGYYG
SALQQDCRKC VCNYLGTVRE DCEGLESCQC EAATGQCRCL PNVVGQTCDR CAPHTWRLAS
GAGCEQCGCD PTRSLGPACN EFTGQCQCMP GFGGRTCQEC QELFWGDPGV ECRACDCNPR
GIQTPQCDRA TGQCICNEGV EGPRCDKCSR GYSGFFPNCV PCHQCFALWD VIISELANRT
QQFLDRANAL KITGVTGPYQ QTLNTLEEKL SEIKTIITQN PAAEPLKNIG NLFEEAEKLT
ADVTVKIADI EENLSALAVK SNSTDTDVSV LETDAKSLDH VVKELAEQLE FIKISDVRGA
LDSITKYFQM SLEAEERVNA STVHPDSTVE LSAQTRQEVE DLINEKEAQF KAKQEEQSRL
LDELAGKLQS LDLSKVAEKT CGTPAGASCA ESECGGLNCR TDDGKKKCGG PGCDGLVTVA
HNAWQKAMDF DRDILSALAE VEQLSRMVSE AKQRADEAKQ NAQEVLLKTN ATKEQVDRSN
EDLRNLIKQI RDFLMQDSAD LDSIEAVANE VLNMEMPSTP QQLQALTEDI RERIESLSDV
EVILQQSAGD IARAEMLLEE AKKASKGATD VKVTADMVKA ALEEAEKAQN AAEKAIKQAD
EDIKGTQDLL TSIESENAAS EETLNNATLR LFELEKSVED LKQKAATNSE NVDNIEEKII
TAKQNAEEVK KVLNTELNDK YKTVEDLIAK KTEESADARR KAGMLQDEAK ALLAQANSKL
QLLKDLENTY ENNQKVLEDK AKQLVELEET VRSLLQTISQ KVAVYSTCL
//
