ID A0A452IJQ7_9SAUR Unreviewed; 1013 AA.
AC A0A452IJQ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000028120.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000028120.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000028120.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A452IJQ7; -.
DR STRING; 38772.ENSGAGP00000028120; -.
DR Ensembl; ENSGAGT00000031953.1; ENSGAGP00000028120.1; ENSGAGG00000020436.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR000859; CUB_dom.
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; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR24046; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR24046:SF3; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF14670; FXa_inhibition; 3.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM01411; Ephrin_rec_like; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1013
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018997818"
FT DOMAIN 31..71
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 114..150
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 350..388
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 823..935
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 354..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1013 AA; 112548 MW; 0E591B9BEFC66822 CRC64;
MGSGRRCSAG AALLLLLLQG QVRAAGLLLP DVDECAQGTD DCHPDAICQN IPKLYKCTCK
VGYSGEGKTC EDIDECDNDF NGGCVHECFN IPGNYRCTCY DGFILAHDGH NCLDTDECMF
NNGGCQHLCV NTMGSYECHC KAGFFLSDNQ HTCIHHSEDG MSCMNKEHGC AHICREAPKG
GVACECRPGF ELARNKMDCI LTCNHGNGGC QHTCEDADDG PICGCHPKYI VHLDGKTCLE
REEVVAEISE SNATAGADVD KRVKRRLIME TCAVNNGGCD RTCKDTSTGV HCSCPIGFTL
QFDGKTCKDI DECQASNGGC DHFCKNTVGS FDCSCKKGFK LLTDEKSCQD IDECSFERTC
DHTCINHPGS FECSCNKGYT LYGFTHCGDI NECSINNGGC QKTCVNTPGD YECQCHSSHK
LHWNKKDCVE IEGSMPDDIS PKVLLSCIKS DGSDRCILNC PSEVHLISGM QDAYTLTCGS
SSQLKKKQQN TNESTCLDTS TIKTSVTFKF NEGKCSLKKT EMFREGLQQI LPDNHNSVME
SFYYVNLKCS SGKQVLGAIS RPMTTKEMFI TVDFELETNQ KEVTDTCDLS CARKRTEKRL
RKTIRTLRKA INREQFHVCL SGMDHEVAEK SPKLLNLQEF CGMGQIHVDN RCASCSVGTY
YDGEQELCVL CPNGTYQDEE GQITCEPCPS PQNPGNQKFA GARDISECGG QCSLGEYSSD
GFKPCLPCPF GTYQPEPGRT SCFPCGGGLT TKYSSASMFQ DCETKVQCSP GHFYNTTTHR
CIRCTVGTYQ PEFGQNYCIS CPGNTTTDFD GSTNITQCKN RHCAGELGDF TGYIESPNYP
GNYPANTECT WIINPPPKRR ILIVVPEIFL PIEDECGDYL VMRKSSSSNS VTTYETCQTY
ERPIAFTSRS KKLWIQFKSN EGNSAKGFQV PYVTYDEDYQ ELIEDIVWDG RLYASENHQE
ILKDKKLIKA LFDVLAHPQN YFKYTAQESR EMFPRSFIRL LRSKVSRFLR PYK
//
