ID A0A2Y9KHP6_ENHLU Unreviewed; 1300 AA.
AC A0A2Y9KHP6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protein HEG homolog 1 isoform X2 {ECO:0000313|RefSeq:XP_022370999.1};
GN Name=LOC111155190 {ECO:0000313|RefSeq:XP_022370999.1};
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_022370999.1};
RN [1] {ECO:0000313|RefSeq:XP_022370999.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022370999.1};
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_022370999.1; XM_022515291.1.
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; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
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 PANTHER; PTHR24037; HEART DEVELOPMENT PROTEIN WITH EGF-LIKE DOMAINS 1; 1.
DR PANTHER; PTHR24037:SF3; PROTEIN HEG HOMOLOG 1; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1167..1192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 944..982
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1300 AA; 137453 MW; 54F4471F019B27B8 CRC64;
MDLSTVVSKE AVRTQIPTKN HTSSDAPENF TPQTEAADAR GRNNSSWKTN FTTSPVGADT
ATALISQSLT RALGTLHLPS SSGSEGRADP SHTESLTSRG SVERGKGLPE EVTVHSQVAA
TWVLGQSPPP ALGMGEEITV LGKRNTSGPA LSWLLFSRTP ASSPPSEPSS ASGSTEELNN
STILPSALAS RRASERVATT LPTGVPRMLP SLTVSLQPLN ETENFPKDSE IARTSVSAHS
SPFEAGLQRN REIIRNPGNG EFIEPSTENG FGLASSRVSV GFWQNDSPTF GGDQLASSSE
AELGSPMSQT EAASRPVPSG RSRDSTARWF LTHSKTSADV TGSSTSYPEV VNASVLTHFS
ASAPQSRGSD RAPGQRNYAE PATELLSSSS SESLDSSAPR GERSTTEDGP GPGGSSEVEE
RTSQAHLPHT SATFTGNGER TLRSLTNAST TSGEVGHSVI VPRETESATQ HGNVTLTGDA
RLVSGSLAAS PALGVTGISY SQVSGMDMEQ GTSSDYTDHT YVSSTFTKGE RALLSITDNS
SSPDLRESST SSTKISNSSL SDSSSSSQAQ TGGRNVSSYD REYAQPSTES LAVRTASVPS
YTPTINRPNT LVLLDTDAAL TRGSSSSSSS LGPPLPLPSV SQSHQLFSSV SPSTRASALP
LQSIPDAPKP MSSSPPPLPV SLTASTPASP SAPQTTLPPS PPTLVLPRAR DTPMTSVQTE
TTALSVAMLP KSQTADPKNQ SNPYPEKVIT ESKPPSPDSL PTEATEAVRV RSTPGIPRPS
TLTESSTQQT LSATSISIPQ TSPALTTTIL QTSHPFIPVS TRAAPMADPT IVQTTAEKQL
LPTSPEIPAP QISTERAVTT ERSQVHGNAT SQSIPLTSVP TSVKGLTPGP GVTEEYSPAS
HLLRTSPLPV THISAAEVLT PKSTTSAAQS STRSPEVLSS PAADVNECLL NPCPPLATCN
NTQGSFTCKC AVGYQLEKGI CSLVRTFVTE FKLKKTFLNT TMEKKADLHE VENEITKTLN
MCFSALPGYT RSTVHASGES NAVVVSLQTT FSLASNVTLF DLADGMQNCA NSCRSSAEVC
QLLGSQRRIF KAGSLCKRKT PECDKETSIC TDLDGVALCQ CKSGYFQFNK MDHSCRACED
GYRLENETCM SCPFGLGGLN CGNPYQLITV VIAAAGGGLL LILGIALIVT CCRKSKNDIS
KLIFKSGDFQ MSPYAEYPKN PRSQEWGREA IEMHENGSTK NLLQMTDVYY SPTSVRNPEL
ERNGLYPAYT GLPGSRHSCI FPGQYNPSFI SDESRRRDYF
//
