ID A0A2Y9TK35_PHYMC Unreviewed; 1728 AA.
AC A0A2Y9TK35;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Latent-transforming growth factor beta-binding protein 2 isoform X1 {ECO:0000313|RefSeq:XP_023989204.1};
GN Name=LTBP2 {ECO:0000313|RefSeq:XP_023989204.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023989204.1};
RN [1] {ECO:0000313|RefSeq:XP_023989204.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023989204.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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_023989204.1; XM_024133436.3.
DR KEGG; pcad:102975282; -.
DR Proteomes; UP000248484; Chromosome 11.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 13.
DR Gene3D; 2.10.25.10; Laminin; 17.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4.
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 InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 14.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 16.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 5.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 11.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS01187; EGF_CA; 5.
DR PROSITE; PS51364; TB; 4.
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}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1728
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016019810"
FT DOMAIN 182..214
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 385..417
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 541..584
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 661..713
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 837..879
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 880..916
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 923..962
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1003..1043
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1086..1126
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1127..1168
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1169..1204
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1210..1251
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1318..1370
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1392..1434
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1435..1470
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1491..1543
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1640..1676
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1681..1725
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 38..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 186..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 204..213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 389..399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 407..416
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1439..1449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1728 AA; 186119 MW; B968AAD105A92A47 CRC64;
MRPPATTRCP GRVLRNPWRS FLPLTLALFV GMGHAQRDPV GSYEPAGRDA SRLRRPGGSH
PAAATAKVYS LFREQNVPVP GLPPAERTQP GWGSPSRPAE AEARRPPRAQ QPRRVQPPAQ
TWRSRALRQQ QSAPRARAPP ALPRLGTTQR PRAARGRLTG RNVCGGQCCP GWTTANSTNH
CIKPVCQPPC QNRGSCSRPQ LCVCRSGFRG ARCEEVIPEE EFDPQNSRLA PRRSAEGSPN
LRRSSAARES TTARARPPAP RPPLDRTLSG LSQTHATQQH VGLSQTVRLY LATAANGQLT
SNALPMGPGP ERKDGAQQAA YLHHPSSSWG LNLTEKIKKI KIVFTPTICK QTCAHGRCAS
SCERGDTTTL YSQSGHGHDP KSGFRIYFCQ IPCLNGGRCI GRDECWCPTN STGKFCHLPT
PNLDREPPER GVRHRASPQG PLKQSTFTLP LSNQMASVSP SLVKVHIHHP PEASVQVHQV
ARVRGEVEAA PEENSVETRP SPWLPASPGH GPWDSNSIPA RSGEVPRPPP QVVPRTPALL
GRCYLSAVNG QCANPLLELT AQEDCCGSVG AFWGVTSCAP CPPRPASPVI ENGQLECPQG
YKRLNLTHCQ DINECLTLGL CEDSDCVNTR GSYLCTCRPG LLLDPSRSRC VSDKAVSMQQ
GPCYRLLGPG TCTLPLAQRI TKQICCCSRV GKAWGSKCEK CPVPGTEAFR EICPAGHGYT
YSSSDIRLSM RKAEEEELTR PLREQGKKSN ATLPRPAERQ PLREATGTWL EAGTTPDKGD
SQAGQVTTSV TQLSAWVPGD ALGRPTPPLP GQGIPEAREE EQVTAPTDVL VTPAPTGIDR
CAAGATNICG PGTCVNLPDG YRCICSPGYR LHPSQAYCTD DDECLGDPCK GRGRCVNHVG
SYSCFCYPGY TLATSGATQE CQDIDECEQP EVCSGGRCTN TEGSYHCECD QGYVMVRKGH
CQDIDECHHP GTCPDGRCVN SPGSYTCLPC EEGYRGQSGS CVDVNECLTP GVCTHGTCIN
LEGSFRCSCE PGYEVTSDEK GCQDVDECAS RASCPTGLCL NTEGSFTCSA CESGYWVNED
GTACEDVDEC EDPQSSCLGG ECKNTAGSYQ CLCPPGFQLA NGTVCEDVDE CVGEEYCAPR
GECLNSHGSF FCLCAPGFAS AEGGASCQDV DECAVTDRCL GGQCVNTEGS FNCLCKTGFQ
PSPESGECVD IDECANDTMC GSHGFCDNTD GSFRCLCDQG FETSPSGWDC VDVNECELML
AVCGAALCEN VEGSFLCLCA SDLEEYDAQE GRCRPRVAGG QKIPEAPPGE HPPGPIRMGC
YSGQKGQPPC SSLLGRNTTQ AECCCTQGTG WGDACELCPA EDSVEFSEIC PSGKGYIPVE
GAWMFGQTTY TDADECVMFG PGLCQNGRCL NTVPGYICLC DPGYHYDAAR RKCEDHDECQ
DMACENGGCM NTEGSFHCFC SPPLTLDLSQ QRCVNSTSGA EDLPDHDIHT DICWKKVTNY
VCSHPLHGRH TTYTECCCQD GEAWSQQCAL CPPRSSEVYA QLCNVARIEA EREAGVHFRP
GYEYGPGPED LHYSLYGPDG VPFYNYLGPE DTIPEPLFPN MASRPGDRTP VLEPPLQPSE
LQPHYVASHP EHQAGFEGLQ AEECGILNGC ENGRCVRVQE GYTCDCFEGF QLDTADMACV
DVNECDDLNG PAALCVHGHC ENTEGSYRCR CPPGHVAEAG PPRCTAKE
//
