ID A0A3Q4N7G8_NEOBR Unreviewed; 1094 AA.
AC A0A3Q4N7G8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Fibulin-2-like {ECO:0000313|Ensembl:ENSNBRP00000028809.1};
GN Name=FBLN2 {ECO:0000313|Ensembl:ENSNBRP00000028809.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000028809.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000028809.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the fibulin family.
CC {ECO:0000256|ARBA:ARBA00006127}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3Q4N7G8; -.
DR STRING; 32507.ENSNBRP00000028809; -.
DR Ensembl; ENSNBRT00000029560.1; ENSNBRP00000028809.1; ENSNBRG00000021897.1.
DR GeneTree; ENSGT00940000156047; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000021897; Expressed in liver and 4 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 5.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 6.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 10.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 4.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 465..497
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 554..591
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 768..806
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 811..852
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 853..891
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 183..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 121681 MW; 23EC93FB7C915EC5 CRC64;
AAWKVFSRHM WGATFTALDL GPNFQWCSPL QRDCTGVDCP VLQNCIENVL EKGACCPKCI
QNGCTCEGYQ YYDCVKAGFR DGKVPEGKSY FVDFGSTECS CPQGGGKISC HFIPCPEISP
NCIDILQPAD GCLQCGRIGC AHGNKKYEAG HSFQIDHCQV CHCPDEGGRL MCSPIPGCDR
RSVNKPMSVT TTENNNPLRD FRGNRNSQQT SLAEPFSKLV RENTLPLYKQ DPPSFGTEDY
DYTLAEPTSS TIQNLAQPLE STTLPPAYPE SSSTSLSSRD ERRHRLQEES PNTQRSTEDE
VTHNMDPTTT GGENKTSSPK ATTATQIVTT GHHRPQQETG ERPMKHGSHR NRVGQDTLRD
TARTAFSFQF LPLIEFTETW KHSPVSSVVT LSGRIVAAGR PQLQSRHFCS HFSCVLFSVR
TAQQQCCLGS LRESRCLAGL NAARAGNMCR EDASCLCELQ ECCTCCSLGL QFRSEGHRCE
AHHYLDFHCK HIFLTCCEGE EGRTVNQDAF RRPLSALRSS CHLLSDSPYR REAFSIGQEQ
NGENAVESPV EVEDMDECLI YEGNICHHIC VNTIGSFRCE CNPGYVLQED TFSCVQGNNI
CEQQCTPVGG QPRCSCSPGF SLRADGRSCE DTNECLSPHA CQLNEHCMNT AGSYVCQRLI
TCPPGYQINN DICEDINECA QRTHNCGDGF ECVNTEGSFR CNPKTRCPVG FSHNMQGRCV
DVDECGALTQ PCSPGFNCVN TMGSYICNRK ITCSRGYHAS PDGSRCVDVD ECQSNVHRCG
EGQLCHNLPG SYRCECRTGY QYDSFRRMCV DINECWSYRG RLCAQTCENT PGSYECSCTS
GFRLSGDGKN CEDVNECLAN LCSQECANVY GSYQCYCRQG YYLKEDGHTC EDIDECSQSI
GHLCTYKCVN IPGSYKCACP DYGYTMSPNG RSCRDIDECA TGANNCSLAE TCYNIQGGYR
CLSFSCSANY RRVSDTRCER ISCPNYLECQ NSPLRITYYY LSFQSNIIIP AQIFRIGPSP
AYSGDNIIVS ITSGNEENYF STRKLNAYTG AVFLNRQVQG PRDFLINVEM KLWRQGTFTT
FHARIYVFIT GNLL
//
