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Database: UniProt
Entry: W5KNT0_ASTMX
LinkDB: W5KNT0_ASTMX
Original site: W5KNT0_ASTMX 
ID   W5KNT0_ASTMX            Unreviewed;      1596 AA.
AC   W5KNT0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Si:ch211-241e1.3 {ECO:0000313|Ensembl:ENSAMXP00000009242.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000009242.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000009242.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted, extracellular space, extracellular matrix, basement membrane
CC       {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   STRING; 7994.ENSAMXP00000009242; -.
DR   Ensembl; ENSAMXT00000009242.2; ENSAMXP00000009242.2; ENSAMXG00000008991.2.
DR   eggNOG; KOG1836; Eukaryota.
DR   GeneTree; ENSGT00940000155638; -.
DR   HOGENOM; CLU_002814_0_0_1; -.
DR   InParanoid; W5KNT0; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000008991; Expressed in zone of skin and 14 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
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; 2.
DR   CDD; cd00110; LamG; 3.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
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; PTHR10574:SF406; LAMININ SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00282; LamG; 3.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   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:UP000018467};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1596
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017303584"
FT   DOMAIN          113..159
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          160..216
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1202..1359
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1400..1571
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          1366..1397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          246..280
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          315..360
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          416..698
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        132..141
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        187..196
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1596 AA;  177745 MW;  EE580BFA2B4A9D2E CRC64;
     MSARCLRIRA LSSGALRLLM ILQLLGLCVA GPRPFHRTPR HPWRDQYPGT QRVQFPSVSD
     RESQRIQIPS LSDMDTQRVQ FPSLSDDNDN AGLVTQRCSR GFYRDRSSRC VPCVCNGLSD
     DCEESTGRCL NCQYNTAGDH CERCKEGYYG SAALRTCKIC PCPLPQTSNN FAVGCTELLS
     GRFQCQCKAG YTGERCERCA PGYYGDPEVF GGRCRPCNCN GNSCSPKTGA CNNGQVPKDI
     DPEVGCQECD NCAQTLLNDL DRLEEELLQI KSDLDNMNSS SSAYIRLKKL EEAIADTKNV
     VTDYGAAVDR LSPKVTELER DALALTGDIK LLNDKAENRS KDAQAAAENI EKTHEKAKAL
     YSQTLDLLAK INELLKLMQN TDWPNGSQPS GDVNKLLAEA ERLVKEMQGR NLKPQNDAAV
     KELDEAQKLL EYVKNNCTKQ YNQNLESATR IKDQLNNYEA KLKELEAALK EASSTVQRAN
     NQNGLNNKTL SDVMEKMKKL QQEKDSVSKE IVLAKQQLNA TEDLLKMLSD SKKEYEQLAA
     QLDGAKTDLT SKINTISQAA AKEGLVKRAE DHAAMLSKLA NDLQQAVKNS SGRTDVQNAL
     SAIDAYRNIT EAVKAAEEAA RRAKEAADKA LNDITQGDVT NRAKDLKDES NRLLKDAKNA
     AKDLKQATED LTNQKQRLDD AERKKDVLKK ELAAINTDLS GIKRDDIGRM IDAAKRTAAD
     ASASANDTLD KLNAIKDEIS KFKATPSSSN VDGLLSDVDM TVKNLSTSIP SLLDKISQVE
     KLSSEIDPNN NISNNINRIK DLIEQARAAA NRIMVPMKFN GDGYVELRAP KDLDDLRAYT
     ALSILLQRPE DSRGDDLRRR RQTSPGRGNL FVLYLGNRDA TKDYIGMALK SNILIFVYKL
     NGKVYEMETD SITPSKGVQS FFDRVDLQRV YQDARIKLTK AFTSTNPPEP QYFEQLGEPL
     QNLLNLDPSE VVFYVGGYPD DFTPPAPLQF PKYKGCIEFS SMNEKFISLY NFKSVKPANT
     TLPEPCKRYF PPSNDYFEGS GYIKANFGAS ALDRVLIFQQ TFESKAQNAL LMYISNETTS
     YWITIERGHF VIRGRVNGKF LQPNITAGTY KLSGDLMVIF QNNERYISVR WKRVAVLQFQ
     YTPESFNTYY IGGIPKELRE RDNISTVPLK GCVSNLEADR SSPTIVERVG VGRGCYPDLQ
     IIRKAEFHSG SSLKTPAGGF DLSGDVALSL GFRSTDNDGV LLQNRQAISK FELTMQNGFV
     MLDFLGSMWK SKKQYQDGEW HYLTVVKNGQ NVEFRIDEDD VGERVTSSTS SANSDLIVLG
     NDLFTGCMSN LYMRRPESMY RPEDFSNFNA DGNVFLDLCD AARPPENMLT NPSQSGSQNE
     KKDQKENNTS SCFTPTPVPH SLRLAGASST LSYTLPTPLS NGLSFSLDVR TKSAEGLLLY
     IPAKQDSYHL ALYVSRGRIR LSMENKGEIF NRETYNDGKW HTVTLSLEKR RYRLVIDGLR
     AQDRVLNPGE VQRGSTQLSS NIYLGTPPPS IHEDLKRKKL PDQAVFGCVR DFKMNDSPMP
     VAAVNRGVGP CFEGHSESGA YFSQGAYVIV GESAIF
//
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