ID A0A1D2NK21_ORCCI Unreviewed; 1330 AA.
AC A0A1D2NK21;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Protein slit {ECO:0000313|EMBL:ODN05623.1};
GN ORFNames=Ocin01_01029 {ECO:0000313|EMBL:ODN05623.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN05623.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN05623.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN05623.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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:ODN05623.1}.
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DR EMBL; LJIJ01000019; ODN05623.1; -; Genomic_DNA.
DR STRING; 48709.A0A1D2NK21; -.
DR OMA; ACAYGFH; -.
DR OrthoDB; 5475408at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 5.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR006207; Cys_knot_C.
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; IPR001791; Laminin_G.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR45836:SF4; PROTEIN SLIT; 1.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01463; LRRCT; 2.
DR Pfam; PF01462; LRRNT; 3.
DR SMART; SM00041; CT; 1.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00368; LRR_RI; 5.
DR SMART; SM00365; LRR_SD22; 9.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF52058; L domain-like; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 6.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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}; Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 774..809
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 811..848
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 850..886
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 888..926
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 928..964
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 975..1012
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1015..1188
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1217..1254
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1253..1330
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 799..808
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 838..847
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 876..885
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 916..925
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 954..963
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 979..989
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1002..1011
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1221..1231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1244..1253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1330 AA; 148598 MW; ACD5EB463052CE09 CRC64;
MLKFASYFKQ LSINTIPPRF SYFEIREDAS IIHLASLSRR SKVCDLSNNH LSAIRKRSLL
GPTSLKSLIL DHNQITCIDE AAIRSLKDLE ILALDHNNLT SLQRDIFEGL TKLKHLTLGD
NPLICDCHLA WLAGWLKSTP RTSSQARCNS PYHLRDKTVD EVMESEFKCA GVIERTWSKC
GGDEECPHPC VCADGVVDCR DLTLKHVPDS LPHDVIELRL EQNEIAEIPP GAFTPYKRLR
RLDLSNNIIQ KIAVDAFRNL KSLTSLLLNA NRITCIRKDT FRDLTNLSLL SLYDNKIQSL
ENGTFESLRN IQTLHLARNP FVCDCRLKWL AEYLHHNPIE TSGAKCESPK RMQRKRLASF
KEDKLKCDDG ESKMAFDECS DTKCPVECVC EGTSVDCSNR GLQEVPKDIP EQVMMLNLSG
NDLSRVRNGW IPTLPHLQKL DLTGNRISAI EDGAFRDSGS LLEVTLTGNK LKEINNKMFV
GLSNLKALSL TDNQITCIMP GSFEHLPNLK SLSLNGNSFI CNCHLAWFGE WLRREESIVS
TDGPKCHAPL RHKDSLIRSL PPHEFRCTSD DRGCLGEGYC PPQCNCTGTV VWCSRAKLRE
IPSGIPPETS ELYLDVNEIQ RIDVGRLGHL KYLTKLDLSN NQVSMISNLT FANLTKLSTL
IISYNKLQCI ERDAFTGLAS LRILSVHAND VSVIPEGTFR DLRSLTHLAL GGNPLFCDCG
LKWLADWVKR DFLEPGIARC SEPETMRSKL LLTTPPGDFE CVDNVPSAIR AKCDACFTFP
CANGASCESL ANRDYQCNCA PGYHGRHCEQ VIDACYGQPC INGGTCRVME EGRFSCTCPP
GFVGHRCETN ENDCLNHKCE NNATCVDLIG QYRCDCQPGF TGEYCEKKIA FCTKEFNPCT
NGAKCIDHFS HYTCECPPGF QGENCSVNVD DCINHMCQNG GTCMDGINEY TCQCTDEFSG
RYCEVLPSVA MLYPKTSPCQ DNDCVHGFCF LPPDSSDYTC KCTPGYSGKR CEILTSISIG
SNGSWVELEP LRTKPEANIT IMLSTYEQNG VLLYNGEGQH IAVELFLGRV RISYDVGNYP
ASTMYSYEMI ADGEEHAIEL LAINKNFTMR VDRGKARSII NDGDRDLLKL TTPLYIGGLP
PTVASTALNQ WHLRNSTSFH GCLSLLIINN KRVDYTNAKR QQGVVPGCAA IQGEEPVSKD
VSAAQIQSTF STKTKVVKDV CKDNRCKHGR CIPSKNGKDY ACRCTPGFGG RFCEQAPTCK
KEQYKDYYTE HGCRSRRPLK IAACIGSCGD TCCTPKRSRR RRVRLICNDG TRYTKDVEII
RKCACSKKCY
//
