ID A0A2Y9KCY5_ENHLU Unreviewed; 1385 AA.
AC A0A2Y9KCY5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Protein HEG homolog 1 isoform X1 {ECO:0000313|RefSeq:XP_022370998.1};
GN Name=LOC111155190 {ECO:0000313|RefSeq:XP_022370998.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022370998.1};
RN [1] {ECO:0000313|RefSeq:XP_022370998.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022370998.1};
RG RefSeq;
RL Submitted (SEP-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_022370998.1; XM_022515290.1.
DR STRING; 391180.A0A2Y9KCY5; -.
DR KEGG; elk:111155190; -.
DR OrthoDB; 5358383at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
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 PANTHER; PTHR24037; HEART DEVELOPMENT PROTEIN WITH EGF-LIKE DOMAINS 1; 1.
DR PANTHER; PTHR24037:SF3; PROTEIN HEG HOMOLOG 1; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1385
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016068622"
FT TRANSMEM 1252..1277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 988..1027
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1029..1067
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 33..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1017..1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1385 AA; 146786 MW; CA405029B49F7145 CRC64;
MASPPLPRPL LLLLPPLLLL LLLPPAAPGT RGWPPSPALR APSGAPLAGA GLARPPEPGP
ERELLPTPPP PTPPRERRGL ASPGPSRTAL GLATAARRGP SRRAPRGGSA DLAWSSWTES
NTESHIENIT FDQNQMDLST VVSKEAVRTQ IPTKNHTSSD APENFTPQTE AADARGRNNS
SWKTNFTTSP VGADTATALI SQSLTRALGT LHLPSSSGSE GRADPSHTES LTSRGSVERG
KGLPEEVTVH SQVAATWVLG QSPPPALGMG EEITVLGKRN TSGPALSWLL FSRTPASSPP
SEPSSASGST EELNNSTILP SALASRRASE RVATTLPTGV PRMLPSLTVS LQPLNETENF
PKDSEIARTS VSAHSSPFEA GLQRNREIIR NPGNGEFIEP STENGFGLAS SRVSVGFWQN
DSPTFGGDQL ASSSEAELGS PMSQTEAASR PVPSGRSRDS TARWFLTHSK TSADVTGSST
SYPEVVNASV LTHFSASAPQ SRGSDRAPGQ RNYAEPATEL LSSSSSESLD SSAPRGERSI
TGISYSQVSG MDMEQGTSSD YTDHTYVSST FTKGERALLS ITDNSSSPDL RESSTSSTKI
SNSSLSDSSS SSQAQTGGRN VSSYDREYAQ PSTESLAVRT ASVPSYTPTI NRPNTLVLLD
TDAALTRGSS SSSSSLGPPL PLPSVSQSHQ LFSSVSPSTR ASALPLQSIP DAPKPMSSSP
PPLPVSLTAS TPASPSAPQT TLPPSPPTLV LPRARDTPMT SVQTETTALS VAMLPKSQTA
DPKNQSNPYP EKVITESKPP SPDSLPTEAT EAVRVRSTPG IPRPSTLTES STQQTLSATS
ISIPQTSPAL TTTILQTSHP FIPVSTRAAP MADPTIVQTT AEKQLLPTSP EIPAPQISTE
RAVTTERSQV HGNATSQSIP LTSVPTSVKG LTPGPGVTEE YSPASHLLRT SPLPVTHISA
AEVLTPKSTT SAAQSSTRSP EVLSSPAAVN SCAVNPCLHD GKCVADPTTS RGYRCRCSPS
WQGDDCSVDV NECLLNPCPP LATCNNTQGS FTCKCAVGYQ LEKGICSLVR TFVTEFKLKK
TFLNTTMEKK ADLHEVENEI TKTLNMCFSA LPGYTRSTVH ASGESNAVVV SLQTTFSLAS
NVTLFDLADG MQNCANSCRS SAEVCQLLGS QRRIFKAGSL CKRKTPECDK ETSICTDLDG
VALCQCKSGY FQFNKMDHSC RACEDGYRLE NETCMSCPFG LGGLNCGNPY QLITVVIAAA
GGGLLLILGI ALIVTCCRKS KNDISKLIFK SGDFQMSPYA EYPKNPRSQE WGREAIEMHE
NGSTKNLLQM TDVYYSPTSV RNPELERNGL YPAYTGLPGS RHSCIFPGQY NPSFISDESR
RRDYF
//