ID A0A1L8I1D3_XENLA Unreviewed; 2898 AA.
AC A0A1L8I1D3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Fibrillin-2 {ECO:0000313|RefSeq:XP_018119620.1};
GN Name=fbn2.L {ECO:0000313|RefSeq:XP_018119620.1,
GN ECO:0000313|Xenbase:XB-GENE-6488367};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018119620.1};
RN [1] {ECO:0000313|RefSeq:XP_018119620.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018119620.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018119620.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the fibrillin family.
CC {ECO:0000256|ARBA:ARBA00008972}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_018119620.1; XM_018264131.2.
DR STRING; 8355.A0A1L8I1D3; -.
DR PaxDb; 8355-A0A1L8I1D3; -.
DR GeneID; 108717258; -.
DR KEGG; xla:108717258; -.
DR AGR; Xenbase:XB-GENE-6488367; -.
DR CTD; 108717258; -.
DR Xenbase; XB-GENE-6488367; fbn2.L.
DR OMA; HQCVACP; -.
DR OrthoDB; 354414at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 108717258; Expressed in egg cell and 13 other cell types or tissues.
DR GO; GO:0001527; C:microfibril; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 27.
DR Gene3D; 2.10.25.10; Laminin; 46.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 9.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR049388; FBN_EGF_N.
DR InterPro; IPR040872; Fibrillin_U_N.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR47333; VON WILLEBRAND FACTOR C AND EGF DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47333:SF1; VON WILLEBRAND FACTOR C AND EGF DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12662; cEGF; 6.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 30.
DR Pfam; PF21364; FBN_EGF_st1; 1.
DR Pfam; PF18193; Fibrillin_U_N; 1.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF00683; TB; 9.
DR PIRSF; PIRSF036312; Fibrillin; 1.
DR SMART; SM00181; EGF; 46.
DR SMART; SM00179; EGF_CA; 44.
DR SUPFAM; SSF57196; EGF/Laminin; 8.
DR SUPFAM; SSF57184; Growth factor receptor domain; 12.
DR SUPFAM; SSF57581; TB module/8-cys domain; 9.
DR PROSITE; PS00010; ASX_HYDROXYL; 42.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 29.
DR PROSITE; PS50026; EGF_3; 40.
DR PROSITE; PS01187; EGF_CA; 17.
DR PROSITE; PS51364; TB; 9.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DISULFID 170..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 188..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 518..528
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 835..845
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1917..1927
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2597..2607
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2898 AA; 313206 MW; F75E3A25797F165F CRC64;
MYAVPSPSPI PGGHRRTVLL LGCVLVLVGC ATVPPAAGQY AFSAESSRGA QEAREGTISA
ANRVRRRGQQ DALRGPNVCG SRFHSYCCPG WKTLPGGNQC IVPICRNSCG DGFCSRPNMC
TCSTGQISPN CGSKTIQQCS VRCMNGGTCV EDHCQCQKGY VGAHCGQPVC ENGCQNGGRC
IGPNRCACVY GFTGPQCERD YRTGPCFTQV SNQMCQGQVT GIVCTKTLCC ATIGRAWGHP
CEMCPAQPQP CRRGFIPNIR SGACQDVDEC QAIPGLCQGG NCINTDGSYE CRCPVGHKQS
ETTQKCEDID ECTTIPGVCN GGECSNTIGS YYCICPRGYV TSGDGSRCVD QRSGVCFSSL
VNGHCAQEQA GRFTKLQCCC ESGRCWALGS LPEMCPIRGT DEYRRLCIEG VPFGGPGGFV
PNGFGPGGTG FGPGGTGFIP GTGGNGFHPG IGGTGIDGQG PVINGGVATL NQTIDICKQY
PNLCLNGRCI PNLNNYRCEC NMGYKQDTQT ECIDVDECTS NPCTNGDCVN TPGSYYCKCH
SGFQRTPTKQ SCIDIDECIQ NGILCKHGRC VNTEGSFQCI CNAGFELTPD GKNCADHDEC
STTNMCLNGM CINEDGSFKC ICKPGFVLAS NGRYCTDIDE CQTPGICMNG HCINTEGSFR
CDCPPGLAIG VDGRVCVDTH MRSTCYGGIK KGLCVRPFPG AVTKSECCCA NPDYGFGEPC
NPCPPRNSAE FQGLCSGGIG ITVDGRDINE CALDPDICAN GICENLRGSF RCNCNSGFES
DSSGKNCIDI DECLVNRLLC DNGLCRNTPG SYSCTCPKGY VFRSDSETCE DINECESSPC
VNGACRNILG SFSCECSPGS KLDSTGLICI DSLKGTCWLN IQDGRCEVNI NGATLKSECC
ATLGAAWGSP CERCEIDTAC PRGFARVKGV SCEDVNECEV FPGVCPNGLC LNTKGSFLCE
CPDGLTLDGT GRLCQDLRME HCFLKWDEDE CVHPVPGKFR LDACCCAVGA AWGTECEECP
KPGSQEFELL CPRGPGFTNR GDVLSGRPFY KDINECKAFP GICTNGKCRN TIGSFKCKCN
NGFALDMEER NCTDIDECRI SPDLCGSGTC INTPGSFECD CFEGFESGFM MMKNCMDIDE
CERNPLLCRG GECINTEGSF LCNCPNGHEL TPSGDACVDI NECALSDNLC RNGKCVNIVG
TYQCSCNPGY QATLDRLGCT DIDECTIMNG GCDTHCTNSE GSYECSCLEG YALMPDKRTC
TDIDECEDNP DICDGGQCSN IPGEYRCLCF DGFMASMDMK TCIDVNECDI NSNICLFGDC
ENTKGSFVCH CQVGYAVKKG TTGCTDVDEC EIDAHNCHLH ATCLNVPGSF KCTCKEGWIG
NGIICNDLDE CLIGTHRCSV SAHCLNTPGS YHCSCAEGYT GDGFTCSDVD ECSENINLCE
NGQCLNIPGS YRCECDMGFT PVPDSRSCQD IDECAFQNIC VFGTCSNLPG MFRCICDEGY
ELDRTGGNCT DVDECADPIN CVNGFCVNTP GRYECNCPPD FQLNPTGVGC VDTRVGNCYL
NHGPRGDGTI SCSTEIGVGV SRSSCCCSLG KAWGNPCEIC PPVNSSEYNT LCPGGEGFRP
NPITIILEDI DECQELPGLC QGGNCINTFG SFQCECPQGY YLSEETRICE DIDECFTQPG
VCGPGTCYNT LGNYTCICPS EYMQVNGGHN CMDMRKSFCY RTYNGTTCDN ELPFNVTKKM
CCCTYNIGKA WSKPCEPCPT PGTANFKNLC GSIPGFTFDI HTGKAVDIDE CKEIPGICTN
GVCINQIGSF RCECPTGFSY NDLLLVCEDI DECSSGDYFC QRNADCINSP GTYRCECSTG
FKLLPNGACI DRNECLEIPN VCSHGTCVDT EGSYHCVCNN GFRVSPDQTM CMDIDECERQ
PCGNGTCKNT VGSYNCLCYP GFEVTHNNDC LDIDECNSFF GQVCRNGHCF NEIGSFICLC
NEGYELTPDG KNCIDINECV AFPGSCSPGT CQNLEGSFRC ICPPGYEVER DHCIDIDECI
EEPNICLFGT CSNTPGSFQC ICPPGFVLSE NGRRCFDTRQ SFCFTRFENG KCSVPKAYNS
TKAKCCCSKM PGEGWGDPCE LCPKEGEVSF QDLCPYGHGT IPGIGDTRED VNECLENPGI
CANGHCINTD GSFRCECPMG YNLDYTGVNC VDTDECSIGN PCGNGTCTNV IGTFECLCDE
GFEPGPMMVC EDINECILNP LLCAFRCINT YGAYECTCPA GYILREDQKM CKDLDECIEG
FHDCESRGMV CKNLIGTFMC ICPLGMVRRP DGEGCMDENE CRTKPGICEN GRCVNTIGSY
RCECNEGFQS TPSGTECLDT RQGFCFAEVL QTMCQMSSSS RNHVTKSECC CNGGRGWGNQ
CEICPLPGTA QYKKMCPHGP GYTTDGKDID ECKVMPNLCR NGQCINNIGS YRCFCNPGYT
TDIGGTACVD LDECSQSPKP CNFICKNTEG SYQCSCPRGY ILQEDGKSCK DLDECQTKQH
NCQFLCVNTI GGFTCKCPLG FTQHHTACID NNECGSQTNL CGPKGVCQNS PGSFTCECQR
GYSLDSTGIN CEDVDECVGT HRCQHGCQNI NGGYRCSCPQ GYIQHYQWNQ CVDENECATP
NTCGSASCFN TLGSYKCACP AGFSFEQFSS ACHDVNECTS SKNPCNYGCS NTEGGYLCGC
PPGYYRVGQG HCVSGIGFNR GQYLSAGIEN SEDNALSPEG CYECQVNGYS KKTGRIKRDA
KNQELERNAN NTELAKNGQI SLKSLDMDLP LKMVLNISHI NSKKHILELL PAIRPLTNHV
RYVISQGNTN MFRINQRDGL SYLHASQKIL PGTYTLEITS IPLYKKNDII ELEQKHEENY
LLGELGESLN IRLQIELI
//
