ID A0A182Q2Z8_9DIPT Unreviewed; 1378 AA.
AC A0A182Q2Z8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein slit {ECO:0008006|Google:ProtNLM};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF002063-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF002063-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF002063-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AXCN02001179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 69004.A0A182Q2Z8; -.
DR EnsemblMetazoa; AFAF002063-RA; AFAF002063-PA; AFAF002063.
DR VEuPathDB; VectorBase:AFAF002063; -.
DR OrthoDB; 5475408at2759; -.
DR Proteomes; UP000075886; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
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; 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; PF00054; Laminin_G_1; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF01463; LRRCT; 4.
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; 6.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 16.
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; 4.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 4.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 824..859
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 861..898
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 900..936
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 938..976
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 978..1014
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1025..1063
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1066..1239
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1264..1301
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1307..1378
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 849..858
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 888..897
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 926..935
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 966..975
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1004..1013
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1029..1039
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1034..1051
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1053..1062
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1291..1300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1378 AA; 154902 MW; 469211A5D4AA8729 CRC64;
MQRQLKNFGY KTKIHRRGTW DLQGNNISVI YESDFQGLAK LRILQLTDNH IYTIEKDALH
DLISLERLDL SQNALTAVPK RAFKGAPALR SLQLDNNQIT CLDEGAVKGL TELEILTLNN
NNITTLPRDM FAGMPRLRAL RLSENPFACD CHLSWLARYL KNASRLAPYT RCHSPGQLKG
QNVADLHEQE FKCSGLTENA PMECGGRSLC PHPCRCADGI VDCREKSLTT VPTTLPEDTT
ELRLEQNYIT EIPPKAFANH RRLKRIDLSN NNISRVAYDA FSGLKSLTSL VLYGNKIKDL
PASVFKGLTS LQLLLLNANE ISCVRRDAFK DLHNLSLLSL YDNNIQSLAN GTFDSLRSIQ
TLHLARNPFI CDCNLRWLGD YLHQNPIETS GARCDAPKRM QRRRIEALKD EKFKCTDDNS
KIKYSGECRM DQECPAACHC DRTTVDCSGR GLREIPRDIP LYTTELLLND NELNRIKSDG
LFGRLPNLSK LDLRRNQISG IEPNAFEGAT KIQELFLSEN KIAEVHNKMF LGLHHLKTLS
LYDNIITCVM PGSFDYLTSL TQLNLASNPF RCNCHLAWFS DWLRKKQLNG PPARCTSPSK
VRDVPIKDLP HFDFKCTSDM DQGCLGEGYC PPSCTCTGTV VRCSRNKLKE IPKSIPPETT
ELYLESNEIS MIHSNRINHL KALTRLDLSN NQIGILSNYT FANLSKLSTL IISYNNLQCV
QKYALSGLTN LKVLSLHGNK ISMIPEGTFN DLQSITHIAL GSNPLYCDCS LRWLSEWVKR
DYVEPGIARC AEPEPMKDKL ILSTPASQFV CAGKVSNEIL SKCDACYTFP CKNDAVCSAL
PERQYECRCK PGYHGTHCEF MIDACYGNPC RNNGTCTVLE EGRFSCHCLQ GYSGSRCEVN
IDDCSDHKCQ NNGTCVDGVN SYSCACAASF TGEYCESKIE FCGKDFNPCQ NGAKCVDHTT
HYSCDCQPGY RGLNCTENID DCVNHMCQNG GTCVDGINDY TCKCPNEFTG KFCEGAPMVA
MMYPQTSPCQ QHECKFGVCF QPNPSSADYV CKCAPGYSGK RCEYLTSLTF LHNNSFVELE
PLRTKPEANV TIVFSSTQQN GVLMYDGHNE HLAVELFNGR IRVSYDVGND PVSTMYSFEM
VADGKYHLVE LLAIKKNFTL RVDRGLARSI INEGTKDYLK LSSPMYLGGL PAEPGQQAYK
QWHLRNLTSF KGCMKEVWIN HKQVDFLNAA RQQKITPGCA LLDQDNEGEM DDDFMQETPV
ILKEVNPCEN HQCKRGGKCV PNGKGGYTCK CKKGTKGKYC DQAANTCRKE QVREYYTEND
CRSRQPLKYA KCIGGCGNQC CAAKVVRRRK VRMVCSNNTK YVKQLDIVRK CHCTKKCY
//
