ID A0A151NQY5_ALLMI Unreviewed; 1369 AA.
AC A0A151NQY5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Slit-like protein 3 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Y1Q_0004884 {ECO:0000313|EMBL:KYO39257.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO39257.1};
RN [1] {ECO:0000313|EMBL:KYO39257.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO39257.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:KYO39257.1}.
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DR EMBL; AKHW03002337; KYO39257.1; -; Genomic_DNA.
DR RefSeq; XP_019342687.1; XM_019487142.1.
DR GeneID; 102558206; -.
DR CTD; 6586; -.
DR OrthoDB; 5475408at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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; 8.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; SLIT HOMOLOG; 1.
DR PANTHER; PTHR45836:SF9; SLIT HOMOLOG 3 PROTEIN; 1.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 2.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00365; LRR_SD22; 5.
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; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 3.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 763..798
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 800..839
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 841..877
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 879..917
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 919..955
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 964..1000
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1003..1177
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1181..1210
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1213..1248
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1253..1289
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1294..1369
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 788..797
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 829..838
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 867..876
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 907..916
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 945..954
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 990..999
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1150..1177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 1200..1209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1217..1227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1238..1247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1257..1267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1279..1288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1369 AA; 151817 MW; 227ABF98C491FAE7 CRC64;
MSKPPPGQLD NNQISCIEDG AFRALRDLEI LTLNNNNITR IPVTSFNHMP KIRTLRLHTN
FLHCDCHLAW LSDWLRQRRT IGQFTFCVTP GNMRGQLVVN VQKKDFVCSG SQSEPPSCSA
SSITCPSACT CSNNVVDCRG RGLTEIPANL PEDIWEIRLE QNFIKAIPPG AFSQYKRLKR
IDISKNQISD IAPDAFKGLK SLNSLVLYGN KITEIPLGLF DDLVSLQLLL LNANKINCLR
VNTFQGLHNL NLLSLYDNKL QTISKGLFAP LRSIETLHLA QNPFVCDCHL KWLADYLKNN
PIETSGARCS NPRRLANKRI GQIKSHKFRC SGSEDFRSKF SGKCFMDLVC PEKCRCEGTI
VDCSNQKLSR LPSYLPEYTT DLRLNDNDIS VLEATGLFKK LSKLRKINLT NNKIKEIREG
TFDGASGVQE LILTQNQLES VHGRMFRGLT GLKTLMLRNN LISCISNDTF AGLSSVRLLS
LYDNHISTLT PGAFNTLVSL STINLLSNPF NCNCHLAWLG KWLMRKRVVS GNPRCQKPFF
LKDIPIQDVD AKDFTCDNND ESSCLLSPPC PAQCTCMDSV VRCSNKGLRI LPKGIPKDVT
ELYLEGNHLT AVPKGLSSFR HLTLIDLSNN SISMLANYTF SNMTQLSTLI LSYNRLRCIP
VHAFNGLKSL RVLTLHGNDI SSVPEGSFND LVSLSHLALG TNPLHCDCSL RWLSEWVKAG
YKEPGIARCS GPDNMVDRLL LTTPTHHFQC KGPIDINIVS KCNPCLSGPC KNNGTCNNDP
VEFYRCTCPS SFKGRDCSMP INACIQNPCQ NGGTCHLTET NKDGFSCSCP LGYEGERCEV
NPDDCEDNDC ENNSTCVDGI NNYVCLCPPN YTGELCDEVI NHCVPELNPC QHESKCLSLA
RGFRCECLPG YSGKHCETDD DDCVGHKCRH GAVCVDAVNG YTCVCPQGFS GLFCENPPPM
VLLQTSPCDN YECQNGAQCI VVHNEPVCRC LAGFAGQKCE KLITVNFVGK DSYVELPSAK
IRPQANISLQ VATDKDNGIL LYKGDNDPLA LELYQGHVRL IYDTVNSPPT TVYSVETVND
GQFHSVELVM LNQTLNLVVD KGTPRSLGKL LKQPSVNLNT PLYIGGIPTS TGLSSLHHGT
DRMPNGFHGC IHDVRINNEL QDFKDLPQQS LGVLPGCKSC NICKHGICRS LEKTSVICEC
HPGWTGPLCD QEIGDPCLNN KCLHGKCIAT NFAYTCKCTE GYSGMYCDKK NNSSNPCRIL
KCNHGQCKFS ERGEPYCECD PNYSGDHCDR ENLCQGEIIR EVIHKEQGYT SCVTTSKVPR
MECHGTCSNG QCCIPLRSKR RKYIFQCADG SSFMEELERH VECGCSKCL
//
