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Database: UniProt
Entry: H0V9J0_CAVPO
LinkDB: H0V9J0_CAVPO
Original site: H0V9J0_CAVPO 
ID   H0V9J0_CAVPO            Unreviewed;      1425 AA.
AC   H0V9J0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Attractin {ECO:0000313|Ensembl:ENSCPOP00000006485.3};
GN   Name=ATRN {ECO:0000313|Ensembl:ENSCPOP00000006485.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000006485.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000006485.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000006485.3};
RG   Ensembl;
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   EMBL; AAKN02012819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02012820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02012821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02012822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 10141.ENSCPOP00000006485; -.
DR   Ensembl; ENSCPOT00000007265.3; ENSCPOP00000006485.3; ENSCPOG00000007193.4.
DR   VEuPathDB; HostDB:ENSCPOG00000007193; -.
DR   eggNOG; KOG1388; Eukaryota.
DR   GeneTree; ENSGT00940000157346; -.
DR   HOGENOM; CLU_003930_0_0_1; -.
DR   InParanoid; H0V9J0; -.
DR   OMA; MNGCPSD; -.
DR   TreeFam; TF321873; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000007193; Expressed in frontal cortex and 12 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0042552; P:myelination; IEA:Ensembl.
DR   GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00055; EGF_Lam; 2.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46376:SF3; ATTRACTIN; 1.
DR   PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF01344; Kelch_1; 2.
DR   Pfam; PF13964; Kelch_6; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF01437; PSI; 2.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00423; PSI; 5.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 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   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1275..1299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          93..126
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          128..244
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          242..279
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          791..915
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1059..1104
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DISULFID        97..107
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        116..125
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        246..256
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        250..267
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        269..278
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1076..1085
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1088..1102
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1425 AA;  158185 MW;  FECB3BAE631D6630 CRC64;
     MVAAAATTEA GLQSRTANIA ALAGKKGGRH RDWNVTRAER PGLGVGLRLL RLLSPSLPPR
     RFLLLLLLLF LLVPWEAEAA AAAAAVSGSA ASEAKECDRP CVNGGRCNPG TGLCVCPTGW
     VGEQCQHCGG RFRLTGSSGF VTDGPGNYKY KTKCTWLIEG QPNRIMRLRF NHFATECSWD
     HLYVYDGDSI YAPLIAAFSG LIVPERDSNE TVPEVVVTSG YALLHFFSDA AYNLTGFNIT
     YNFDMCPNNC SGRGVCKISN SSNTVECECS ENWTGESCDI PYCTDNCGFP HRGICNSSNV
     RGCSCLSEWQ GPGCSVPVPA NQSFWTREEY SNLKLPRASH KAVVNGNTMW IVGGYMFNHS
     DYNMVLAYDL VSKEWLPLNR SVNNVVVRYG HSLALYKDKI YMYGGKIDST GNVTNELRVF
     HIHNESWVLL TPKAKEQYAV VGHSAHIVTL NTGRVVMLVI FGHCPLYGYI SNVQEYDLDK
     NTWSILPTQG ALVQGGYGHS SVYDHKTKAL YVHGGYKAFS ANKYRLTDDL YRYDVDTQMW
     TILKDSRFFR YLHTAVVVSG TMLVFGGNTH NDTSMSHGAK CFSSDFMAYD IACDRWSVLP
     RPDLHHDVNR FGHSAVLHNS TMYVFGGFNS LLLSDILVFT SEQCESHQSE AACIAAGPGI
     RCVWDTETSQ CVSWELTTEE QVIKLKSECV SKGTLDHDRC DQNTDCYSCT ANTNDCHWCN
     DHCVPRNHSC TEGQISIFKY ENCPKDNPMY YCNKKTSCRS CALDQNCQWE PRNQECIALP
     ENICGMGWHL VGNVCLKITT AKENYDNAKL SCRNHNAFLA SLTTQKKVEF VLKQLRMMQS
     SQTMSKLTLT PWVGLRKINV SYWCWEDMSP FTNSLLQWMP SEPSDAGFCG ILSEPSNRGL
     KAATCINPLN GSVCERPANH SAKQCRTPCA LRTACGECTS SSSECMWCSN MKQCVDSNAY
     VASFPFGQCM EWYTMSSCPP ENCSGYCTCS HCLEQPGCGW CTDPSNTGKG KCIEGSYKGP
     VKMPSQASTG IVYPQPLLNS SMCLEDGRYN WSFIHCPACQ CNGHSKCINQ SICEKCENLT
     TGKHCETCIS GYYGDPTNGG KCQPCKCNGH ASLCNTNTGK CFCTTKGVKG DECQLCEVEN
     RYQGNPLKGT CYYTLLIDYQ FTFSLSQEDD RYYTAINFVA TPDEQNRDLD MFINASKNFN
     LNITWAASFS AGTQAGEEMP VVSKTNIKEY KDSFSNEKFD FRNHPNITFF VYVSNFTWPV
     KIQIAFSQHS NFMDLVQFFV TFFSCFLSLL LVAAVVWKIK QSCWASRRRE QLLREMQQMA
     SRPFASVNVA LETDEEPPDL IGGSVKTVPK PIALEPCFGN KAAVLSVFVR LPRGLGGIPP
     PGQSGLAVAS ALVDISQQMP IVYKEKSGAV RNRKQQPPAQ PGTCI
//
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