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Database: UniProt
Entry: A0A2K6QHZ4_RHIRO
LinkDB: A0A2K6QHZ4_RHIRO
Original site: A0A2K6QHZ4_RHIRO 
ID   A0A2K6QHZ4_RHIRO        Unreviewed;      1753 AA.
AC   A0A2K6QHZ4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Deleted in malignant brain tumors 1 protein {ECO:0000256|ARBA:ARBA00014650};
DE   AltName: Full=Hensin {ECO:0000256|ARBA:ARBA00030560};
GN   Name=DMBT1 {ECO:0000313|Ensembl:ENSRROP00000028395.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000028395.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000028395.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the DMBT1 family.
CC       {ECO:0000256|ARBA:ARBA00009931}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   Ensembl; ENSRROT00000052746.1; ENSRROP00000028395.1; ENSRROG00000037950.1.
DR   GeneTree; ENSGT00950000183145; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 9.
DR   Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR   Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR042235; ZP-C.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48071:SF15; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00530; SRCR; 9.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00202; SR; 9.
DR   SMART; SM00241; ZP; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF56487; SRCR-like; 9.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS00420; SRCR_1; 7.
DR   PROSITE; PS50287; SRCR_2; 9.
DR   PROSITE; PS00682; ZP_1; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   3: Inferred from homology;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1753
FT                   /note="Deleted in malignant brain tumors 1 protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014455324"
FT   DOMAIN          103..203
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          234..334
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          355..455
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          463..563
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          593..693
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          722..822
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          853..953
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          984..1084
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          1110..1221
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          1227..1330
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          1352..1461
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          1470..1721
FT                   /note="ZP"
FT                   /evidence="ECO:0000259|PROSITE:PS51034"
FT   DISULFID        128..192
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        141..202
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        172..182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        259..323
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        272..333
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        303..313
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        380..444
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        393..454
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        424..434
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        488..552
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        501..562
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        532..542
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        618..682
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        631..692
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        662..672
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        747..811
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        760..821
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        791..801
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        878..942
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        891..952
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        922..932
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        1009..1073
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        1022..1083
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        1053..1063
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        1255..1319
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        1268..1329
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        1299..1309
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ   SEQUENCE   1753 AA;  190093 MW;  24F1FF2F2F6EB9A0 CRC64;
     MGISTVILEM CLLWGQVLPT GEWIPSTTDY GSLIPLEASL EVTSEEVSPF PSEAPLGSTR
     VLEGSVFPSE TPLGSTVAEG SVFPSETPLG STVAEGSDYG LALRLVNGGD RCQGRVEVLY
     QGSWGTVCDD SWDTNDANVV CRQLGCGWAT SAPGNARFGQ GSGSIVLDDV RCSGYESYLW
     SCPHNGWLSH NCGHSEDAGV ICTAAQPQST LRPDSWPVRI SPVPTEGSES SLALRLVNGG
     NRCQGRVEVL YRGSWGTVCD DSWDTSDANV VCRQLGCGWA TSAPGNARFG QGSGPIVLDD
     VRCSGHESYL WSCPHSGWLS HNCQHSEDAG VICSDALPTT TLPASTVGPE SSLALRLVNG
     GDRCQGRVEV LYRGSWGTVC DDSWDTNDAN VVCRQLGCGW ATSAPGNARF GQGSGPIVLD
     DVRCSGNESY LWNCPHRGWL SHNCGHGEDA GVICSGPESS LALRLVNGAN RCQGRVEVLY
     RGSWGTVCDD YWDTNDANVV CRQLDCGWAT SAPGNARFGQ GSGPIVLDDV RCSGHESYLW
     SCPHSGWLSH NCGHGEDAGV ICSAAQSRLA RPDTLSTSTL PASTVGSESS LAVRLVNGSD
     RCQGRVEVLY RGSWGTVCDD SWDTSDANVV CRQLGCGWAT SAPGNARFGQ GSGPIVLDDV
     RCSGQESYLW SCPHRGWLSH NCGHHEDAGV ICSVSQSQST PGPDTWPISR ASTAGSESSL
     ALRLVNGGDR YQGRVEVLYR GSWGTVCDDS WDTNDANVVC RQLGCGWATS APGNARFGQG
     SGPIVLDDVG CSGHESYLWN CPHRGWLSHN CGHSEDAGVI CSAAQSQSTP RPDTWLTTNL
     LTSPIGSESS LALRLVNGGD RCQGRVEVLY RGSWGTVCDD SWDTNDANVV CRQLGCGWAT
     SAPGNARFGQ GSGPIVLDDV GCSGHESYLW NCPHRGWLSH NCGHSEDAGV ICSAAQSQST
     PRPDALLTTN LLTSPIGSES SLALRLVNGG DRCQGRVEVL YRGSWGTVCD DSWDTNDANV
     VCRQLGCGWA TSAPGNARFG QGSGPIVLDD VGCSGHESYL WNCPHRGWLS HNCGHSEDAG
     VICSATQINS TTTDWWHPTT TTTTRPSSNC GGFLFSASGT FSSPSYPAYY PNNAKCVWEI
     EVNSGYRINL GFSNLQLEVQ YNCSFDYVEI FDGSLNSSHL LGKICNDTRQ IFTSSYNRMT
     IHFRSDISFQ NTGFLAWYNS FPSDATLRLV NLNSSYRLCA GRVEIYHGGT WGTVCDDSWT
     IHEAEVVCRQ LGCGRAVSAL GNAYFGAGSG PITLDDVECS GTESTLWQCR NRGWFSHNCR
     HNEDAGVICS GNPLSTPAPF LSITSPNTNY SCGGFLSQPS GDFSSPFYPR NYPNNAKCVW
     DIKVQNNHRV TVIFRDVQLE GGCNYDYVEV FDGPYHSSPL IARVCDGARG SFTSSSNFMS
     IRFVSDHSIT RRGFRAEYYS SPSNDSTNLL CLPNHMQASV SRSYLQSLGF SAHDLVISTW
     NGYYECRSQI TPSLVIFTIP YSGCGTIKQA DNDTIDYSNF LTAAHVAPSR GIITRRKNFR
     IHVSCRMLQN TWVDTMYIAN DTIQVEEVQY GNFDVNVSFY TSSSFLYPVT SHPYYVKLNQ
     DLYVQAEILH SDAALTLFVD TCVASPYSND FTSLNYDLIR SGCVRDDTYG PYSQPSPHIA
     RFRFRAFHFL NRFPSVYLHC KMVVCRAYDP SSRCNRGCVM RSKRDVGSYQ EKVDVVLGPI
     QLQTPPRLEE EPQ
//
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