ID G1U0E3_RABIT Unreviewed; 2456 AA.
AC G1U0E3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Eyes shut homolog {ECO:0008006|Google:ProtNLM};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000022823.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000022823.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000022823.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000022823.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000022823.3};
RG Ensembl;
RL Submitted (NOV-2023) 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; AAGW02018528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9986.ENSOCUP00000022823; -.
DR PaxDb; 9986-ENSOCUP00000022823; -.
DR Ensembl; ENSOCUT00000028796.3; ENSOCUP00000022823.3; ENSOCUG00000015539.4.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000164728; -.
DR HOGENOM; CLU_006496_0_0_1; -.
DR InParanoid; G1U0E3; -.
DR TreeFam; TF343620; -.
DR Proteomes; UP000001811; Chromosome 12.
DR Bgee; ENSOCUG00000015539; Expressed in testis.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045595; P:regulation of cell differentiation; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 14.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.10.25.10; Laminin; 19.
DR InterPro; IPR013320; ConA-like_dom_sf.
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 PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF00008; EGF; 7.
DR Pfam; PF12661; hEGF; 6.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 16.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 8.
DR PROSITE; PS00022; EGF_1; 17.
DR PROSITE; PS01186; EGF_2; 13.
DR PROSITE; PS50026; EGF_3; 21.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 15..51
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 53..92
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 105..141
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 143..179
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 181..219
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 221..259
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 261..297
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 299..335
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 337..373
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 375..411
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 413..448
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 450..486
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 489..526
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 528..564
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1211..1393
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1429..1470
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1475..1674
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1670..1703
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1706..1743
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1754..1944
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1945..1981
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1983..2024
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2039..2217
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2218..2254
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2255..2292
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2297..2456
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 131..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 169..178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 190..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 209..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 249..258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 287..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 325..334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 363..372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 401..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 417..427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 438..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 476..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 516..525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 554..563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1460..1469
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1733..1742
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1971..1980
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2014..2023
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2190..2217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 2244..2253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2282..2291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2456 AA; 270612 MW; 56A114D8F6A9490D CRC64;
MFLFSFHIGL LCEINRKKCD FSPWLHNSTS AELKERFKCI CHPGFIGKYS EIDTDKCASR
PCKNGATCID QQSNYFCQCM PPFKVIAGFS CLCSPGHAGL RCEHDIDDCL LHACEHNATC
EDLHLSYQCV CQSGWEGHFC EQESNECKMN PCENNSTCTD LYKSYRCDCK SGWTGKNCSE
EINECDSDPC MNGALCHESI VPGQFICLCP PFYMGQFCHQ RYNTCDLIND TCRNNSTCLT
LVDGNHCICR EGFLGDHCEI DVNECLSLPC QNYGDCEDGV NEFRCVCRPG FSGHLCEIEI
NECSSKPCKN NGTCVDLENS FLCNCQPGYH GSFCELTGNE CKTSSCAEAE NCVSTSGEDS
CICGPGYTGS DCEVNIDECL SEPCLHDGDC IDGVNHYTCD CKSGFFGTHC ETNANDCFSN
PCQHGRCIDL INAYQCLCDA EWTSTRCEVK ITDCSSITCM NEGFCQESIH GFTCICPLGY
TGAYCEKSFE PEMNLVLCLN GGIRVDGPEH NFDCRCLSGF SGQFCEINID ECSSSPCLHG
ANCEDHINGY ICICQQGWSG HHCEKEVYEC IDNSCTAIYK DEPGSSYFYT SESVTCSIGL
LHDDEMSRVT CLLPISQRTD VTSSQTYIIL PSETSVSSSP SVRATAIWTT MDTYPADQGK
DIFKHDVPPT IELISSKELS AKQSLSFLSH KTSVSQLSIQ TSVAMPTFFF PDRRKTPLMG
SSLLTDFTFP TQSFLLERYQ TAALFATTMN SVISDIAGAA TELNRHSLLS RGFTLSTAST
SAPPVVSRGA EEGIEKYSAV SLISRIQHWR LLSSSMSPIL PAKIIISKQV AILNSSTLHR
FSTQASLSSE HHAITEASSD RRLTNINSQA ADSLSELSQT CATCSMTEIK SSYEFSDQVL
HRKQSHFYET FWMNSAILAS WYALMGTQTI TSGHAFSSPT EITPSVAFTE LSSLFPSKKS
AKGTILSSSL EESITLSSNL DVNLCLYKTC LSIVPSQTVS SDFMNSDLTS QLTTDDLSLS
ENILKLLKIG QYPVAVAPTG ILSQGNVKDI EEGGVPHTHI KHHRSDNSLD LELSLQTDSS
VTLKINTETV RSNDFKNRLP LPTDSLSDFA QIFSNVALYT ISAPQPLPVQ TSFPTSVSQP
SSPFYMDYPP FTSDLKEQGR TAVDWPRWEL QPSMQDRQSL AASQGPSITR PLTLSSLESL
TAPQQLIVSD FSCIRYYGDS YLKFQNVFLN QQNSISLEFQ TSSSYGLLLY VKQDSDSVDK
FFTQLFVENG TLKYQFFCAG DAELKSINTT IRVDNGQKYT LLIRQELDPC KAELTILERI
IKFSETTHPL SGKPLPISGS VFIGGSPHLH GKDQISGPVS MENFTGCIEV IEFNNLRSFI
PSKAVEKYHI DNCRSQDLAL SPATTFIAPS GTTQGNDSRP TSLGPSPAAP SVCQETTCHH
GGTCRPIFLS SGSYAFQCDC PLRFTGRFCE KDAGLLFPSF NGNSYLELPF FTNLDDMKFI
LEKKHNRIVT IYLTIKTSSL NGTILYSTDS NFGEQFLHLF LVEGRPTVKY GCGSSQNILT
VSANYTINRN AFIPITIRYT VPIGSPEVTC MIEMAAGGEP PMQKKNIETT YTQGYFESMF
LGSIPGNVKI SKSVGQIFGF EGCIRELQVN NKEVLIIQEA LHGKNIENCY IPWCDHHLCH
NNGTCISDGE NWFCECPRLY SGQLCQFSIC ENNPCGNGAT CVPKSGTDIV CLCPYGRSGP
LCTDAINITQ PRFSGTDASG YTSFLAYSRI SDISFNYEFH LKFQLANNHS SLQNNLIFFT
GQKGHGLNGD DFLSVGLLDG CVVYSYNLGS GIASIRSEPL DLSLKIHTVY LGRFFRKGWL
KVDDHQNKSI ISPGRLIGLN VFSQFYVGGY SEYLPDLLPD GASFKNGFQG CIFTLQVRTE
KDSHFRGLGN PEGRPIAGRT VGQCDASPCS LMKCGNGGTC IEDGAVVYCK CPTGWKGTFC
TQAVSTCDPE HDPPHHCSKG ATCVSLPHGY TCYCPLGTTG IYCEQVFSLP FPSAFSISDP
SFRSDELSWM SFAPFQIRKK THIQLQFQPL AMEGILFYVA QHLKAQSGDF LCLSLVKGSV
QLRYNLGDRT IILENPQKIT ANGSIWHMIK AGRVGAEGYL EVDGMNITEK ASAKMSSLDT
NTDFYVGGLS SLNLVNPMAT ANEPAGFQGC VREVIINNQE LQLTELGAKD GSNVGDCDGT
ACGYSTCRNG GECMVNGTAF SCRCLPHWTG NTCNESVHCL NNPCLHQSLC IPDRSFSYSC
LCTLGWVGRH CENKTSFSTA KFMGNSYIKY SDPNYKERNL QFTTISLNFS TTETEGLIVW
MGKAQNEEND FLAIGLHNQT LRIAVNLGGK ISVSMSYSNV TFCCNKWHHV AVNQNQTLIT
AYLDNSLILS KDIDSHKTFV ALNYGGICYL GGFEYGRKVS IITQEIFKRD FVVTCC
//
