ID A0A7J8JUQ6_MOLMO Unreviewed; 302 AA.
AC A0A7J8JUQ6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE SubName: Full=Fibrillin 1 {ECO:0000313|EMBL:KAF6500049.1};
GN ORFNames=HJG59_005009 {ECO:0000313|EMBL:KAF6500049.1};
OS Molossus molossus (Pallas' mastiff bat) (Vespertilio molossus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Molossidae;
OC Molossus.
OX NCBI_TaxID=27622 {ECO:0000313|EMBL:KAF6500049.1, ECO:0000313|Proteomes:UP000550707};
RN [1] {ECO:0000313|EMBL:KAF6500049.1, ECO:0000313|Proteomes:UP000550707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMolMol1 {ECO:0000313|EMBL:KAF6500049.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6500049.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6500049.1}.
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DR EMBL; JACASF010000001; KAF6500049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8JUQ6; -.
DR Proteomes; UP000550707; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR FunFam; 2.10.25.10:FF:000097; Fibrillin 2; 1.
DR FunFam; 2.10.25.10:FF:000103; Fibrillin 2; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR049388; FBN_EGF_N.
DR InterPro; IPR040872; Fibrillin_U_N.
DR InterPro; IPR051145; GAS-SHBG-PROS.
DR InterPro; IPR017878; TB_dom.
DR PANTHER; PTHR24040:SF8; FIBRILLIN 1; 1.
DR PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF21364; EGF_FBN_1st; 1.
DR Pfam; PF18193; Fibrillin_U_N; 1.
DR SMART; SM00181; EGF; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51364; TB; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000550707};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..302
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029532447"
FT DOMAIN 146..178
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 184..212
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DISULFID 150..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 168..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 302 AA; 31969 MW; 3D8D33AE011811E1 CRC64;
MRRGRLLEVA LGFTVLVASY TSYGADTNLE VGNVKETRAS RAKRRGGGGH DALKGPNVCG
SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC TCPSGQISPS CGSRSIQHCN
IRCMNGGSCS DDHCICQKGY MGTHCGQPVC DSGCLNGGRC VAPNRCACTY GFTGPQCERD
YRTGPCFTVV SNQMCQGQLS GIVCTKTLCC ATTSTNVKLE HTTATDTPYV PTQQEASNAA
AAMGGLEMAL SAQIWTNAPM EPTRAVRMQT ARTPWAPTAA SARKATRAMA SLAQISMSAP
RI
//
