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Database: UniProt
Entry: A0A1A6HUD6_NEOLE
LinkDB: A0A1A6HUD6_NEOLE
Original site: A0A1A6HUD6_NEOLE 
ID   A0A1A6HUD6_NEOLE        Unreviewed;      1205 AA.
AC   A0A1A6HUD6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS01186};
DE   Flags: Fragment;
GN   ORFNames=A6R68_24171 {ECO:0000313|EMBL:OBS81839.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS81839.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS81839.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS81839.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS81839.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the LDLR family.
CC       {ECO:0000256|ARBA:ARBA00009939}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:OBS81839.1}.
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DR   EMBL; LZPO01009017; OBS81839.1; -; Genomic_DNA.
DR   STRING; 56216.A0A1A6HUD6; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00112; LDLa; 11.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR22722:SF11; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2; 1.
DR   PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00057; Ldl_recept_a; 11.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00192; LDLa; 11.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 11.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS01209; LDLRA_1; 5.
DR   PROSITE; PS50068; LDLRA_2; 11.
DR   PROSITE; PS51120; LDLRB; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          93..108
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01186"
FT   DOMAIN          134..149
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01186"
FT   REPEAT          197..239
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          346..389
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          666..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        545..557
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        552..570
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        586..598
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        593..611
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        627..639
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        634..652
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        748..763
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        774..786
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        781..799
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        793..808
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        813..825
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        820..838
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        832..847
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        852..864
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        859..877
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        871..886
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        896..908
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        903..921
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        945..963
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        982..994
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        989..1007
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OBS81839.1"
FT   NON_TER         1205
FT                   /evidence="ECO:0000313|EMBL:OBS81839.1"
SQ   SEQUENCE   1205 AA;  135276 MW;  9E2A62A2547647AC CRC64;
     SLEIALLPSL PVEMTDLRTG GAFPGLGSVM AIQTVLTPLM SYRTAPGEPA LEENSPAPNS
     VYLGDFRSIN ECLDSSISRC DHNCTDTITS FYCSCLPGYK LMSDKRTCVD IDECKESPQL
     CSQKCENVIG SYICKCXPGY IREPDGKTCR QNSNIEPYLI FSNRYYLRNL TTDGAFYSLI
     LQGLGNVVAL DFDRVEKRLY WIDTEKQIIE RMFLNKTNRE TIVRHRLLRA ESLAVDWVSR
     AHARLAVYVG TLGLQKYTAV PLLFVAFEKL YWLDAVLDCL FVSDLEGRHR KMLAQHCVDA
     NNTFCFENPR GIVLHPQNGY CPSVILYPSP CIHSPVHVAA YGRETLHVYW ADWGSRAYIA
     RVGMDGANKS VIISTKIEWP NAITIDYTND LLFSDLDGHH RQTVYDGTLP HPFAITIFED
     TVYWTDWNTR TVEKGNKYDG SDRAVLDFEK QQRTTIVNNP CGTNNGGCSH LCLIKAGGKG
     FTCECPDDFQ IVHLRGQTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC LDGSDEPDLC
     PHRFCRLGQF QCRDGNCTSP QALCNAHQDC ADGSDEDHGL CDHHRCESNQ WQCANRRCIP
     EAWQCDSVND CQDNSDEDSL RCASRTCKPG QFRCNNGRCI PQSWKCDVDN DCGDYSDEPI
     HECSEFPGGS HAKPELGGKQ MAPPPQPKGR GTTSNRDACR QRLFSGYVVN IDRPCPLYNH
     MSAAYNCDNH TEFSCKTNYR CIPQWAVCNG ADDCRDNSDE QDCGRKGSRE ALPCTPGNFR
     CRNHHCIPLR WKCDAYDDCG DNSDEENCVP RECTESEFRC VDQQCIPSRW VCDQENDCGD
     NSDERDCEMK TCHPEHFQCA SGHCVPSSLA CDGRADCLDA SDESSCPTRF PNGTYCPAAM
     FECKNHVCIQ SFWICDGEND CVDGSDEELH LCFNVPCESP HRFRCDNSRC IYGHQLCNGV
     DDCGDGTDEK EEHCKNPTHK PCTETEYKCT NGHCISEHYV CDNVDDCGDL SDETDLGENR
     TCAENICEQN CTQLSNGGFI CSCSPGFKSS TLDKNSCQDI NECEQFGICP QSCRNSKGSY
     ECFCADGFKS MSSHYGERCA ADANPPLLLL PENVRIRKYN VSSEKFSEYL EEEEHIQALD
     YDWDPEGMDL SVVYYTVLGQ GSEFGAIKRA YIPDFESGSN NPMRAVDLGL KYIMQPDGLA
     VDWVG
//
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