ID A0A1A6HJI1_NEOLE Unreviewed; 663 AA.
AC A0A1A6HJI1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Suppressor of tumorigenicity 14 protein homolog {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=A6R68_19192 {ECO:0000313|EMBL:OBS78421.1};
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:OBS78421.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS78421.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS78421.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS78421.1};
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:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
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:OBS78421.1}.
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DR EMBL; LZPO01027433; OBS78421.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6HJI1; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 5..119
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 63..134
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 170..277
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 423..662
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 289..307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 301..316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 326..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 349..361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 356..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 368..383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OBS78421.1"
FT NON_TER 663
FT /evidence="ECO:0000313|EMBL:OBS78421.1"
SQ SEQUENCE 663 AA; 73518 MW; 4AA449676A0A5D35 CRC64;
SNVRVQKVFN GHLRVTNENF LDAYENSNST EFKSLANQVK EALKQLYSEV PVLGPYYKRS
DSCHFALHAH GGEVTRFTTP GFPNSPYPAH ARCHWVLRGD ANSVLSLTFR SFDVAPCDEH
GSDLVIVYDA LSPMEQHAVN VFLVTLITST DRRHPGFEAT FFQLPKMSSC GGSLSDAQGI
FSSPYYPGHY PPNIDCTWNI KVPNNRNVKV RFKLFYLVDP NVPLGTCTKD YVEINGVRYC
GERSQFVVSS NSSKITVHFH SDHSYTDTGF LAEYLSYDSN DPCPGMFMCN TGRCIRRDLR
CDGWADCPDY XDENHCRCNT TXQFMCKNKF CKPLFWVCDN VNDCGDGSCP ADSFKCSNGK
CLPQSQQCDG KDNCGDGSDE ASCDSVNVVS CTKNTYRCQN GLCLSKGNPE YCGLRSFTKQ
ARVVGGTNAD EGEWPWQVSL HALGQGHLCG ASLISPNWLV SAAHCFMDDR NFKYSDHTKW
TAFLGLLDQS KRSSSGVQEH KLKRIITHPS FNDFTFDYDI ALLELEKAAE YSTVVRPICL
PDTTHVFPAG KAIWVTGWGH TQEGGTGALI LQKGEIRVIN QTTCEGLMPQ QITPRMMCVG
FLSGGVDSCQ GDSGGPLSSV ETDGRIFQAG VVSWGEGCAQ RNKPGVYTRL PVLRDWIKDQ
TGV
//