ID G3TP53_LOXAF Unreviewed; 2153 AA.
AC G3TP53;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Tectorin alpha {ECO:0000313|Ensembl:ENSLAFP00000017125.2};
GN Name=TECTA {ECO:0000313|Ensembl:ENSLAFP00000017125.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017125.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000017125.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017125.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000017125.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017125.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSLAFT00000022130.2; ENSLAFP00000017125.2; ENSLAFG00000022861.2.
DR GeneTree; ENSGT00950000183155; -.
DR HOGENOM; CLU_001423_0_0_1; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd19941; TIL; 3.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR025615; TILa_dom.
DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR46160:SF3; ALPHA-TECTORIN; 1.
DR PANTHER; PTHR46160; ALPHA-TECTORIN-RELATED; 1.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF01826; TIL; 3.
DR Pfam; PF12714; TILa; 2.
DR Pfam; PF00094; VWD; 4.
DR Pfam; PF00100; Zona_pellucida; 1.
DR SMART; SM00832; C8; 4.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00215; VWC_out; 3.
DR SMART; SM00216; VWD; 4.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57567; Serine protease inhibitors; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS51233; VWFD; 4.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2153
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003455280"
FT DOMAIN 98..251
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 319..499
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 709..884
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1096..1276
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1483..1664
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1803..2057
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
SQ SEQUENCE 2153 AA; 239503 MW; D8EB066D3EF63972 CRC64;
MNYSSLLRIW VSFIFALVRH QAQPRELMYP FWQNDTKTPK VDDGSSSEIK LAIPVFFFGI
PYRTVYVNNN GVVSFNVLVS QFTPESFPLT DGRAFIAPFW ADVHNGIRGE IYYRETMDPA
ILKRATKDIR KYFKDMGTFS ATWVFIVTWE EVTFYGGSST TPVNTFQAVL VSDGSYTFTL
FNYYEINWTT GTASGGDPTG LGGVMAQAGF NGGNLTNFFS LPGSRTPDIV NIQETTNVNV
PGRWAFKVDG KEIDPANGCT SRGQFLRRGE VFWDDLNCTI KCRCLDFNNE IYCQEASCSP
YEMCEPKGKF FYCSPVETST CVVFGEPHYH TFDGFLFHFQ GSCAYLLARQ CLQTSSLPFF
SVEAKNEHRS GSAVSWVKEL SVEVNGYKVL IPKGSYGKVK VNDLVTSLPV TLELGAVKIY
QSGMSTAVET DFGLLVTFDG QHYASISIPG SYINSTCGLC GNYNKNPLDD FLRPDGRPAM
SVLDLGESWR VYHPDWKCDS GCVDNCTQCD AATEAVYFGS DYCGFLNKTD SPLWECGTVV
DPTAFIHSCV YDLCSVQDNG TLLCQAIQPT PWCPTLGIAI GDWRIQXXSV STVQCPSFSH
YSVCTSSCPN TCSDLTASQN CPTPCTEGCE CNEGFVLSTS QCVPLHKCGC DFDGHYYTMG
EFFWATANCT VQCLCEEGGD VYCFNKTCRS GEVCAVEDGY QGCFPSRETV CLLSQNQVLH
TFDGVAYSFP SEFSYTLLKT CPDRPEYLEI DINKKKPDAG LAWLRGLRIL VADQEVKIGG
VGASEVKLNS QEVELPFFHP SGKLEIYRNK NSTTVESKGV VTVQYADTGL LYIRLSTTYF
DCTGGLCGFF NANASDEFCL PNGKCTDNLA AFLESWTTFE EICNGECGDL LKACSNDSEL
LKFYRSRSRC GIINDPSNSS FLECHGVVNV TAYYRTCLFR LCQSGGNESE LCDSVARYAG
ACKNADVEVG PWRTYDFCPL ECPENSHFEE CMTCTETCET LALGPICVDS CSEGCQCDEG
YALQGSQCVT RSECGCNFEG HQLATNETFW VDLDCQIFCY CNGTDNSVHC ETIPCRADEY
CTEEGGLYYC QARTDASCIV SGYGHYLTFD GYPFDFQTSC PFILCTTGNR PSSDTIPKFI
VTAKNEDRDP SLALWVKQVD VTLFGYSIVI HRAYKHTVLV NNERLYLPLK LGQGKINIFS
FGFHVVVETD FGLKIVYDWK TFLSITVPRS MQNSTYGLCG RYNGNADDDL EMPMGLLASS
VSEFGQSWVK RDIFCQVGCG DRCLSCAKVE GFSKVQQLCS LIPNQNAGFA KCHSKVNPTF
FYKNCLFDSC IDAGAVQTAC SWLQNYASTC QTQGIAVTGW RNYTSCSVTC PPNSHYESCV
SVCQPRCAAI RLKSDCNHYC VEGCQCDVGY VLNGKSCILP HNCGCYSDGK YYEPKQLFWN
SDCTRRCRCF RRNLIQCDPR QCKSEEECAL RNGVRGCFST KASYCLAAGG GVFRTFDGAF
LRFPANCAFV LSTICQKLPD ISFQLIINFD KWSSPNLTII SPVYFYINEE QILINDRNTV
KVNGTQVNVP FITGLATKIY SSEGFLVIDT SPDIQIYYNG FNVIKISISE RLQNKVCGLC
GNFNGDLTDD YVTLRGKPVV SSVVLAQSWK TNGMQKRPLV PSCNELQFSQ YAAMCDNVHI
QKMQGDGYCL KLTDMKGFFQ PCYGLLDPLP FYESCYLDGC YNLKKFQLCG SLAAYGEACR
SFGILSTEWI EKENCSGVVE DPCVGVDCPN RTCELENGGE LCGCIEPPPY GNNSRDIIDV
EVTCKAAQME VSISKCRLFQ LGFEREGVRI NDRRCTGIEG EDFISFQINN TKESCGNIVQ
SNGTHIIYKN TIWIESANNT GNIITRDRTI SVEFSCAYEL DIKISLDSVV KPMLSVINLT
VPTQEGSFTT KMALYKNASY KHPYRQGEVV LTTRDVLYVG VFVVGADATH LILTLNKCYA
TPSRDPNDKL RYFIIEGGCQ NIKDNTIVIE ENGVSLTCRF HVTVFKFIGD YDEVHLHCAV
SLCDTEKQSC KISCPQNSRI ATDYRKEPKE QIISVGPIRR KRLDWCEDNG GCEQICTSQV
DGALCSCVTG TLQEDGKSCR ASNSSVELQV WMILLIMTQI SLWHFVYTTG ITS
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