ID A0A2Y9JA28_ENHLU Unreviewed; 2763 AA.
AC A0A2Y9JA28;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Thyroglobulin {ECO:0000256|ARBA:ARBA00017326};
GN Name=LOC111146558 {ECO:0000313|RefSeq:XP_022357853.1};
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_022357853.1};
RN [1] {ECO:0000313|RefSeq:XP_022357853.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022357853.1};
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:PRU00500}.
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DR RefSeq; XP_022357853.1; XM_022502145.1.
DR STRING; 391180.A0A2Y9JA28; -.
DR KEGG; elk:111146558; -.
DR OrthoDB; 5314395at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00191; TY; 7.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 10.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR14093; HLA CLASS II GAMMA CHAIN; 1.
DR PANTHER; PTHR14093:SF19; THYROGLOBULIN; 1.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00086; Thyroglobulin_1; 8.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00211; TY; 10.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 11.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 6.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 10.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Hormone {ECO:0000256|ARBA:ARBA00022702};
KW Iodination {ECO:0000256|ARBA:ARBA00022653};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Thyroid hormone {ECO:0000256|ARBA:ARBA00022920};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2763
FT /note="Thyroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016160557"
FT DOMAIN 31..92
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 93..164
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 298..358
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 603..656
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 657..728
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 739..920
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1009..1072
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1073..1144
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1145..1209
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1512..1566
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2736..2763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 63..70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 72..92
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 131..138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 338..358
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 636..656
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1041..1048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1180..1187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1189..1209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 2763 AA; 302219 MW; DB53EE9A992F10E5 CRC64;
MALALWVFSL LGSACVASAN IFEYQVDAQP LRPCELQRET TFLRGADHVP QCAEDGSYQT
IQCRNDGGSC WCVDADGREV PGSRQPARPV ACPSFCQLEK QQILLNGYIN GTTAAYLPRC
QASGDYAPVQ CDLGQEQCWC VDAEGMEVYG TRQLGRPTWC PRSCEIRNRR LLHGVGDKSP
PQCSPDGGFL PVQCQFVNTT DMMIFDLIQS YSRFPDAFVT FSAFRSKFPE VSGYCHCADS
QGRELAETGL ELLLDEIYDT IFAGLDLAPT FAETTLYRTL QRRFLAVRLV VSGRFRCPTK
CEVERFTANR FGHPYVPSCR RDGGYQEVQC QRGGPCWCVD ARGKEIHGTR RRGPRPSCAE
DQFCISERRQ ALSRLHFGPS GYFSQHNLFV AQEGRWTSPR VAKFSTSCPP LIKELFVDSG
ILHPMVEGQD KQFPALETLL REAIGAIFPS RELARLALQF TTGPKRLQQN LFGGKFLVNV
GQFNLSGALG TKGTFNFSQF FQQFGLPGFQ NGGTHLAKPL SLGLDSNPAT EPPEASKKGD
ATNRLIVDSF GFEINLQENQ NALTFLASLL ELPEFLLFLQ QALSVPEDIA RDLGDVMEMV
LSSQGCEQTP GSLFVPLCSA EGNYEDVQCF AGECWCVDSR GKELAGSRVR GARPRCPTEC
EKERALMQSL SGSLPAGASL FVPSCNSEGH FLPVQCFNSE CYCVDAEGQA IPGTRSVPGE
LKRCPTPCQL QAEQAFLGVA RALGSDSSVL PSLSSSYVPQ CSASGQWRPV QCDGPPEQAF
EWYERWGAQN NSGQELTPPE LLRKITSYRE AASRSFRLFI QSLYEAGQQG IFPGLARYPS
FQDVPLAVME GNLTQAGGNI LLEPYLFWQI INGQLSRYPG PYSDFSVPLA HLDLRSCWCV
NEAGHELEGT RTAPSEVPAC PGSCEMVKLR VLKFIKETEE IVLASNSSWF PLGESFLAAK
GIWLTNEELS LPQLSPPRET FSEKFLSGGD YAIRLAAQST LDFYQRRGFL PGESTRAAAL
LWPGPYVPQC DVWGGWEPMQ CHAGTGYCWC VDGKGEYVPA SLTARSPQVP QCPTACETSR
ATGLLSSWKQ AVSQGNPSPE DLFIPTCLET GEFARLQELE AGRWCVDPAS GVGTPPSMNN
SVPCPSLCEV LPSGVPSRRA SSGSAPACRA EDGGFSPVQC DPARGICWCV LDSGEEVPGT
RVAGSQPACE SPQCPLPFST PDVAGGVILC ERASGAGGAP IQRCRLLCRP GYRSAFLPGP
LVCSLEEQRW VSQPPQPHTC QRPQLWQTLQ TQGQFQLRLP PGKMCSADYA GLLLAFQVFI
LDELVARGFC QIQAKTFGTP VSIPVCDGST VQVECLTGER LGVNVTWKVP LKDVPPASLP
DLHDIEEVLV GKDLIGRFTD LIQSGGFQLH LDSKIFPADT SIYFLQGDHF GTSPRTWFGC
LEGFHQVLAT SNDTQDPLGC VKCPEGSYFQ KDICIPCPVG FYQEQAGSMA CVSCPLGRTT
ISPGAFSHMH CVTECQKSEE GLWCDQNGQY QASQRNKDSG KAFCVDGEGR RLLWSEMEAP
LSDSQCLMMR KFEKVPESQV ILGANVTAVG RSKVPGSESP LLQCLTDCAL DKTCSFLAVS
TVGSEVSCDF YAWTSDNIAC ITSAQHQDTL GNSKATGFGS LKCRVTVRSR AQGSPAVYLK
KGQEFTTVSQ KSFEQTGFQN TLSGMYGPVV FPGSGADLTG AHLFCLLACD RDSCCDGFIL
AQIQGGPIIC GLLSSPDVLL CNVKDWRDPA EAQANATCPG VTYDQGGRQG TLHLGGLEFQ
IPASVEGPPD TITSFQQVYL WKDSDMGSRS ESLGCGRNME PRPVSPTDTD LATDLFSPVD
LNQVTVNGSR SLPIQQHWLF KHVFSPQQAN LWCLSRCVQE SSFCQLAEIT DNAPLYFTCV
LYPEAQVCND VVESNPKGCR LILPHRPKTL FRKKVVLRDK VKNFYTRLPF QTLTGISIRN
KVPMSEKSIS NGFFECERLC DVDPCCTGFG FLNVSQSKGG EVTCLTLNSL GFQMCTEENG
GAWRILDCGS SDTEVRTYPF GWYEKPVAQD DAPSFCPPVV LPSLPEKVTL DSWQSLAPSA
AVLDPSIRTF DVAHISSAAT SNFSDARDFC LLECSRHPAC LVTTLQTRPG AVRCVFYADA
QICTHSLQAQ NCRLLLREEA THIYRKLNMP LLGFGTLAPS VTIAPHGRLL GRSRAIQVGS
SWKQVDQFLG VPYAAPPLAE SRFQAPEPSN WTGSWDATQP RASCWQPGTQ APAATRVSED
CLYLNMFVPQ NVAPNASVLV FFHNTVEWRG TEGQLALDGS FPAAIGNLIV VTASYRVGVF
GFLSSGSGEV SGNWGLLDQW AALTWVQTHI GVFGGDPRRV TLAADRGGAD VASIHLLTTR
TTDSRLFRRV VLMGGSVFSP AAVISQERAQ QQVAAFAEEV SCPASPIQEM VSCLRQKPAS
VLNDAQTKLL AVSGPFHYWG PVVDGWYLRE APARALQRTP RVKVDLLIGS SQDDGLINRA
KAVKQFEENQ GRTSSKTAFY QALQNSLGGE DADAGVRAAA TWYYSLEHST DDYASFSRAL
ENATRDYFIT CPVIDMASHW ARRAWGNVFM YHAPESYGHS SLDLLADVQY AFGLPFYPAY
QGQFTLEEKS LSLKIMQFFS NFIRSGNPNY PHEFSRKAPE FAVPWPDFIP RAGGENYKEL
SVLLPNRQGL KSTDCSFWSK YIQSLKAAAA DEAKQELSAQ SEEEDGLVNL GLTGEPGSKS
YTK
//
