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Database: UniProt
Entry: A0A087RKY6_APTFO
LinkDB: A0A087RKY6_APTFO
Original site: A0A087RKY6_APTFO 
ID   A0A087RKY6_APTFO        Unreviewed;      1829 AA.
AC   A0A087RKY6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Laminin subunit alpha-4 {ECO:0000313|EMBL:KFM14140.1};
DE   Flags: Fragment;
GN   ORFNames=AS27_05570 {ECO:0000313|EMBL:KFM14140.1};
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:KFM14140.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM14140.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM14140.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL226414; KFM14140.1; -; Genomic_DNA.
DR   STRING; 9233.A0A087RKY6; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
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: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; 3.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.10.25.10; Laminin; 3.
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:SF49; AXOTACTIN; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00282; LamG; 5.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
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:UP000053286};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1829
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001828715"
FT   DOMAIN          84..133
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          134..188
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          189..242
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          840..1041
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1053..1232
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1239..1407
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1476..1647
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1654..1827
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          1418..1455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          441..468
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1431..1446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        103..112
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        159..168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        214..223
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        226..240
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   NON_TER         1829
FT                   /evidence="ECO:0000313|EMBL:KFM14140.1"
SQ   SEQUENCE   1829 AA;  202879 MW;  1B8F4840F0039693 CRC64;
     MALISAWPLV SPILFFLRCF SSSTASSEGG VFQFDIEGSS AVSVQEATVI RGQQQAVATG
     SWVPFAEGCQ EGFYRTSLGK CSPCNCNGNA NRCLDGSGIC VDCQRNTTGQ HCEQCPDGFI
     GDVVRGVPTF CQPCPCPLPA LANFAVSCYR KSGSVRCVCK ENYAGPNCER CAPGYYGNPL
     LIGSTCKKCD CSGNSDPNLI FEDCDEVTGQ CRNCLRNTTG FKCERCAPGY YGDARFAKNC
     TECNCGGRMC DSQTGECLAD SPEVSTGTDC PTISCDKCIW DLTDDIRLAV LAIDESKSTL
     LSISTGVAAQ KRLNDLNLTA THLQVRTLMT FYFLIQPFTS NTSVNTTLYD KWTFTCLSGE
     SKMCGNEASS KGLLVQKETM ETNNRATQLL QQLSNMRDNI EEISSKMKYY AIQQELSPEE
     IAQKLSAAEE MLKEIKRRKP FTNQRQLADE EENAAEELVQ QVEEFHKRYN DTRSLVSDVL
     EQLSEQDVKL SEVEEALDQA LDYVIQTEDI NKENTANLQR REKQHETIKE QIDEVNGILL
     SARTILAGPQ KVNSELSEVI KNVSGFYAEI DGAKKELQEK LANLSLFDDD LVEKAMHHAH
     NLRRLADELD RNLYGVDTNG LVQRAINASN VYENIASYIE EANKAALLAL NTTNRVNDAA
     VGIDTQIIYH KGKSEELLNR ATELQRTADD SNDLTIADTS RHVNGTLARM NALRSQLTRA
     ITKMQSAEPV EARERLEQGK LKTAEAVSAT MTVMQATTPM DENVRLWSQN LQDFQHNSVA
     YDSAVHSAGD AVKKLTEVFP QLLDKLRRVE QKAPANNISS SIQRIRELIA QTRSVASKVQ
     VSMMFGGQSA VEVNPKINVE ELKSFTSMSL YIKLQKDNPQ LAASPDRFIL YLGNKNAKNY
     IGLAIKNDNL VYIYNLGGQD VEIPLDAKPV STWPSYFSII KIERIGRHGK MFLTVPSLSS
     TAEEKFIKKG EVLGPGSLLN LEPENTVFYV GGVPPGFTLP PSLNLPGFIG CLELATLNDD
     VISLYNFKHV YNIDTTTSPP CARNKLAFTQ SRAVSYFFDG SGYALARNIE RRGRFSQVTR
     FDIEVRTPTD NGLILLMING SMFFSLEMHN GFLYLRYDFG FSTGPVLLED SMKKAQINDA
     KFHEISIIYH NSKKMILVVD RRHIKSVDNE RTAMPFTDIY IGGAPTEILH SSISSHLAGS
     IGFKGCMKGF QFQKKDFNLL EEPGTLGISY GCPEDSLMSR KAYFNGESFI ASSQKVSLFS
     EFEGGFNFRT LQPNGLLFYY SEGSDVLSIS MDRGAVVLNA SGTKIQSPDR NYNDGKTHFI
     ITSVTPERYE LTVDDKKQSK KNPAKDRAGK SLDSIKKFYF GGSPLRTQQA NFTGCISNAY
     FTRLDRDVEV EDFQQYPEKV QTSLYGCPVE SPPVALLHKK GKNSSKAKGN RNKKVGRDKD
     KISQTSTGLK KLHQDVNMQR DPQCHLPMNP KATEHAYQFG GTANSRQEFD HIPKDFSERA
     QFSISLKTHS SHGMIFYISD QKETNFMALF VAHGRLIFMF NAGHQKIRIK SQEKYNDGLW
     HNVIFIRGKN IGRLIIDGLR VLEESFGSNA NTWQVTEPLY IGGVAPGKAV KNIQINSVYS
     FSGCLSNLQL NGRSITSASQ TFSVTPCFEG PSEAGTYFSS EGGYVVLDES FSLGLKFEVV
     FEIRPRSSSG ILLHGHSVNG EYLNMHMRNG QVTVKLNNGI RDFSTSVTLK QSLCDGRWHR
     IAVIRDANVV QLDVDSEVNH VVGPLNPKAT DHREPVFIGG VPESLLTSSL TTRNSFIGCI
     RNFMIDEKPV SFSKAALVSG AVSINTCPA
//
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