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Database: UniProt
Entry: A0A2U3XZ44_LEPWE
LinkDB: A0A2U3XZ44_LEPWE
Original site: A0A2U3XZ44_LEPWE 
ID   A0A2U3XZ44_LEPWE        Unreviewed;       383 AA.
AC   A0A2U3XZ44;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Protein delta homolog 2 {ECO:0000313|RefSeq:XP_006736737.1, ECO:0000313|RefSeq:XP_030887490.1};
GN   Name=DLK2 {ECO:0000313|RefSeq:XP_006736737.1,
GN   ECO:0000313|RefSeq:XP_030887490.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006736737.1};
RN   [1] {ECO:0000313|RefSeq:XP_006736737.1, ECO:0000313|RefSeq:XP_030887490.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006736737.1,
RC   ECO:0000313|RefSeq:XP_030887490.1};
RG   RefSeq;
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   RefSeq; XP_006736737.1; XM_006736674.1.
DR   RefSeq; XP_030887490.1; XM_031031630.1.
DR   STRING; 9713.A0A2U3XZ44; -.
DR   GeneID; 102735176; -.
DR   KEGG; lww:102735176; -.
DR   CTD; 65989; -.
DR   OrthoDB; 5475408at2759; -.
DR   Proteomes; UP000245341; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 4.
DR   Gene3D; 2.10.25.10; Laminin; 5.
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   PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF19; PROTEIN CRUMBS HOMOLOG 2; 1.
DR   Pfam; PF21700; DL-JAG_EGF-like; 1.
DR   Pfam; PF00008; EGF; 3.
DR   Pfam; PF12661; hEGF; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..383
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041069103"
FT   TRANSMEM        307..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..58
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          91..129
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          131..172
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          174..210
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          212..248
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        48..57
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        119..128
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        162..171
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        200..209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        238..247
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   383 AA;  40401 MW;  4EC0E381AC07E764 CRC64;
     MPSGCRCLHL VCLLCILGAP VQPARADDCS SHCDLAHGCC APDGSCRCDP GWEGLHCERC
     VRMPGCQHGT CHQPWQCICH TGWAGKFCDK DEHICTTQTP CRNGGQCVYD GGGKYHCVCP
     PGFHGRDCER KAGPCEQAGS PCRNGGQCQD DQGFALNFTC RCLAGFVGAR CEVNVDDCLM
     RPCANGATCL DGINRFSCLC PEGFAGRFCT INLDDCASRP CQRGARCRDR VHDFDCLCPS
     GYGGKTCELI LPVPDAATTA DVPPGPTPAV VVPATGPAPH SVGAGLLRIS VKEVVRRQEA
     GLGASSLVAV VVFGALTAAL VLSTMLLTLR AWRRGVCPPG PCCCPAPHYA PARQDQECQV
     SMLPAGLPLS PDLPLEPGKT TAL
//
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